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P16112

- PGCA_HUMAN

UniProt

P16112 - PGCA_HUMAN

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Protein

Aggrecan core protein

Gene

ACAN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei392 – 3932Cleavage; by aggrecanase
Metal bindingi2266 – 22661Calcium 1By similarity
Metal bindingi2270 – 22701Calcium 1By similarity
Metal bindingi2270 – 22701Calcium 3By similarity
Metal bindingi2290 – 22901Calcium 2By similarity
Metal bindingi2292 – 22921Calcium 2By similarity
Metal bindingi2293 – 22931Calcium 1By similarity
Metal bindingi2299 – 22991Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi2299 – 22991Calcium 2By similarity
Metal bindingi2300 – 23001Calcium 1By similarity
Metal bindingi2300 – 23001Calcium 3By similarity
Metal bindingi2313 – 23131Calcium 2By similarity
Metal bindingi2314 – 23141Calcium 2By similarity
Metal bindingi2314 – 23141Calcium 2; via carbonyl oxygenBy similarity

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. extracellular matrix structural constituent Source: UniProtKB
  3. hyaluronic acid binding Source: InterPro
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. cell adhesion Source: InterPro
  3. extracellular matrix disassembly Source: Reactome
  4. extracellular matrix organization Source: Reactome
  5. glycosaminoglycan metabolic process Source: Reactome
  6. keratan sulfate biosynthetic process Source: Reactome
  7. keratan sulfate catabolic process Source: Reactome
  8. keratan sulfate metabolic process Source: Reactome
  9. proteolysis Source: UniProtKB
  10. skeletal system development Source: UniProtKB
  11. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Ligandi

Calcium, Lectin, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_121120. Keratan sulfate biosynthesis.
REACT_121313. Keratan sulfate degradation.
REACT_163906. ECM proteoglycans.
REACT_267635. Defective B4GALT1 causes B4GALT1-CDG (CDG-2d).
REACT_267713. Defective CHST6 causes MCDC1.

Names & Taxonomyi

Protein namesi
Recommended 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:
Gene namesi
Name:ACAN
Synonyms:AGC1, CSPG1, MSK16
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:319. ACAN.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. Golgi lumen Source: Reactome
  3. lysosomal lumen Source: Reactome
  4. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2266 – 22661D → N in SEMD-ACAN; creates a functional N-glycosylation site; does not adversely affect protein trafficking and secretion. 1 Publication
VAR_063053
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2303 – 23031V → M in OD. 1 Publication
VAR_063765

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

MIMi165800. phenotype.
608361. phenotype.
612813. phenotype.
Orphaneti251262. Familial osteochondritis dissecans.
171866. Spondyloepimetaphyseal dysplasia, aggrecan type.
93283. Spondyloepiphyseal dysplasia, Kimberley type.
PharmGKBiPA24616.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16161 PublicationAdd
BLAST
Chaini17 – 24152399Aggrecan core proteinPRO_0000017505Add
BLAST
Chaini393 – 24152023Aggrecan core protein 2PRO_0000017506Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi51 ↔ 133By similarity
Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi175 ↔ 246By similarity
Disulfide bondi199 ↔ 220By similarity
Glycosylationi239 – 2391N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi273 ↔ 348By similarity
Disulfide bondi297 ↔ 318By similarity
Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi371 – 3711O-linked (Xyl...) (keratan sulfate)1 Publication
Glycosylationi376 – 3761O-linked (Xyl...) (keratan sulfate)1 Publication
Glycosylationi387 – 3871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi434 – 4341N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi500 ↔ 571By similarity
Disulfide bondi524 ↔ 545By similarity
Disulfide bondi598 ↔ 672By similarity
Glycosylationi602 – 6021N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi621 ↔ 642By similarity
Glycosylationi657 – 6571N-linked (GlcNAc...)1 Publication
Glycosylationi737 – 7371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1898 – 18981N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2168 ↔ 2178By similarity
Disulfide bondi2173 ↔ 2187By similarity
Disulfide bondi2189 ↔ 2198By similarity
Disulfide bondi2205 ↔ 2216By similarity
Disulfide bondi2233 ↔ 2325By similarity
Disulfide bondi2301 ↔ 2317By similarity
Disulfide bondi2332 ↔ 2375By similarity
Disulfide bondi2361 ↔ 2388By similarity

Post-translational modificationi

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.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Proteoglycan

Proteomic databases

PaxDbiP16112.
PRIDEiP16112.

PTM databases

PhosphoSiteiP16112.

Miscellaneous databases

PMAP-CutDBP16112.

Expressioni

Tissue specificityi

Restricted to cartilages.1 Publication

Developmental stagei

Expression was detected in chondrocytes throughout the developing skeleton.

Gene expression databases

CleanExiHS_ACAN.
GenevestigatoriP16112.

Organism-specific databases

HPAiCAB016377.

Interactioni

Subunit structurei

Interacts with FBLN1 (By similarity). Interacts with COMP.By similarity1 Publication

Protein-protein interaction databases

IntActiP16112. 1 interaction.
STRINGi9606.ENSP00000268134.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MD4X-ray1.95C89-103[»]
ProteinModelPortaliP16112.
SMRiP16112. Positions 31-135, 154-247, 263-349, 479-572, 588-673, 2165-2200, 2203-2369.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 147114Ig-like V-typeAdd
BLAST
Domaini153 – 24896Link 1PROSITE-ProRule annotationAdd
BLAST
Domaini254 – 35097Link 2PROSITE-ProRule annotationAdd
BLAST
Domaini478 – 57396Link 3PROSITE-ProRule annotationAdd
BLAST
Domaini579 – 67496Link 4PROSITE-ProRule annotationAdd
BLAST
Repeati772 – 77761-1
Repeati778 – 78361-2
Repeati784 – 78961-3
Repeati790 – 79561-4
Repeati796 – 80161-5
Repeati802 – 80761-6
Repeati808 – 81361-7; approximate
Repeati814 – 81961-8; approximate
Repeati820 – 82561-9
Repeati826 – 83161-10; approximate
Repeati832 – 83761-11
Repeati838 – 84361-12
Repeati941 – 959192-1Add
BLAST
Repeati960 – 978192-2Add
BLAST
Repeati979 – 997192-3Add
BLAST
Repeati998 – 1016192-4Add
BLAST
Repeati1017 – 1035192-5Add
BLAST
Repeati1036 – 1054192-6Add
BLAST
Repeati1055 – 1073192-7Add
BLAST
Repeati1074 – 1092192-8Add
BLAST
Repeati1093 – 1111192-9Add
BLAST
Repeati1112 – 1130192-10Add
BLAST
Repeati1131 – 1149192-11Add
BLAST
Repeati1150 – 1168192-12Add
BLAST
Repeati1169 – 1187192-13Add
BLAST
Repeati1188 – 1206192-14Add
BLAST
Repeati1207 – 1225192-15Add
BLAST
Repeati1226 – 1244192-16Add
BLAST
Repeati1245 – 1263192-17Add
BLAST
Repeati1264 – 1282192-18Add
BLAST
Repeati1283 – 1301192-19Add
BLAST
Repeati1302 – 1320192-20Add
BLAST
Repeati1321 – 1339192-21Add
BLAST
Repeati1340 – 1358192-22Add
BLAST
Repeati1360 – 1378192-23Add
BLAST
Repeati1379 – 1397192-24Add
BLAST
Repeati1398 – 1416192-25Add
BLAST
Repeati1418 – 1436192-26Add
BLAST
Repeati1439 – 1457192-27; approximateAdd
BLAST
Repeati1459 – 1477192-28Add
BLAST
Repeati1479 – 1497192-29Add
BLAST
Domaini2164 – 219936EGF-likePROSITE-ProRule annotationAdd
BLAST
Domaini2201 – 2327127C-type lectinPROSITE-ProRule annotationAdd
BLAST
Domaini2330 – 239061SushiPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 14194G1-AAdd
BLAST
Regioni152 – 24796G1-BAdd
BLAST
Regioni253 – 34997G1-B'Add
BLAST
Regioni477 – 57195G2-BAdd
BLAST
Regioni578 – 67295G2-B'Add
BLAST
Regioni676 – 848173KSAdd
BLAST
Regioni772 – 8437212 X 6 AA approximate tandem repeats of E-[GVE]-P-[SFY]-[APT]-[TSP]Add
BLAST
Regioni851 – 1497647CS-1Add
BLAST
Regioni941 – 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-GAdd
BLAST
Regioni1498 – 2162665CS-2Add
BLAST
Regioni2163 – 2415253G3Add
BLAST

Domaini

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.

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation
Contains 1 EGF-like domain.PROSITE-ProRule annotation
Contains 4 Link domains.PROSITE-ProRule annotation
Contains 1 Sushi (CCP/SCR) domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Immunoglobulin domain, Repeat, Signal, Sushi

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000168421.
HOVERGENiHBG007982.
InParanoidiP16112.
PhylomeDBiP16112.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.10.100.10. 5 hits.
InterProiIPR001304. 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]
PfamiPF00008. EGF. 1 hit.
PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 1 hit.
PF07686. V-set. 1 hit.
PF00193. Xlink. 4 hits.
[Graphical view]
PRINTSiPR01265. LINKMODULE.
SMARTiSM00032. CCP. 1 hit.
SM00034. CLECT. 1 hit.
SM00181. EGF. 1 hit.
SM00409. IG. 1 hit.
SM00445. LINK. 4 hits.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 5 hits.
SSF57535. SSF57535. 1 hit.
PROSITEiPS00615. 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]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P16112-1) [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
MTTLLWVFVT LRVITAAVTV ETSDHDNSLS VSIPQPSPLR VLLGTSLTIP
60 70 80 90 100
CYFIDPMHPV TTAPSTAPLA PRIKWSRVSK EKEVVLLVAT EGRVRVNSAY
110 120 130 140 150
QDKVSLPNYP AIPSDATLEV QSLRSNDSGV YRCEVMHGIE DSEATLEVVV
160 170 180 190 200
KGIVFHYRAI STRYTLDFDR AQRACLQNSA IIATPEQLQA AYEDGFHQCD
210 220 230 240 250
AGWLADQTVR YPIHTPREGC YGDKDEFPGV RTYGIRDTNE TYDVYCFAEE
260 270 280 290 300
MEGEVFYATS PEKFTFQEAA NECRRLGARL ATTGHVYLAW QAGMDMCSAG
310 320 330 340 350
WLADRSVRYP ISKARPNCGG NLLGVRTVYV HANQTGYPDP SSRYDAICYT
360 370 380 390 400
GEDFVDIPEN FFGVGGEEDI TVQTVTWPDM ELPLPRNITE GEARGSVILT
410 420 430 440 450
VKPIFEVSPS PLEPEEPFTF APEIGATAFA EVENETGEAT RPWGFPTPGL
460 470 480 490 500
GPATAFTSED LVVQVTAVPG QPHLPGGVVF HYRPGPTRYS LTFEEAQQAC
510 520 530 540 550
PGTGAVIASP EQLQAAYEAG YEQCDAGWLR DQTVRYPIVS PRTPCVGDKD
560 570 580 590 600
SSPGVRTYGV RPSTETYDVY CFVDRLEGEV FFATRLEQFT FQEALEFCES
610 620 630 640 650
HNATATTGQL YAAWSRGLDK CYAGWLADGS LRYPIVTPRP ACGGDKPGVR
660 670 680 690 700
TVYLYPNQTG LPDPLSRHHA FCFRGISAVP SPGEEEGGTP TSPSGVEEWI
710 720 730 740 750
VTQVVPGVAA VPVEEETTAV PSGETTAILE FTTEPENQTE WEPAYTPVGT
760 770 780 790 800
SPLPGILPTW PPTGAETEES TEGPSATEVP SASEEPSPSE VPFPSEEPSP
810 820 830 840 850
SEEPFPSVRP FPSVELFPSE EPFPSKEPSP SEEPSASEEP YTPSPPEPSW
860 870 880 890 900
TELPSSGEES GAPDVSGDFT GSGDVSGHLD FSGQLSGDRA SGLPSGDLDS
910 920 930 940 950
SGLTSTVGSG LTVESGLPSG DEERIEWPST PTVGELPSGA EILEGSASGV
960 970 980 990 1000
GDLSGLPSGE VLETSASGVG DLSGLPSGEV LETTAPGVED ISGLPSGEVL
1010 1020 1030 1040 1050
ETTAPGVEDI SGLPSGEVLE TTAPGVEDIS GLPSGEVLET TAPGVEDISG
1060 1070 1080 1090 1100
LPSGEVLETT APGVEDISGL PSGEVLETAA PGVEDISGLP SGEVLETAAP
1110 1120 1130 1140 1150
GVEDISGLPS GEVLETAAPG VEDISGLPSG EVLETAAPGV EDISGLPSGE
1160 1170 1180 1190 1200
VLETAAPGVE DISGLPSGEV LETAAPGVED ISGLPSGEVL ETAAPGVEDI
1210 1220 1230 1240 1250
SGLPSGEVLE TAAPGVEDIS GLPSGEVLET AAPGVEDISG LPSGEVLETA
1260 1270 1280 1290 1300
APGVEDISGL PSGEVLETAA PGVEDISGLP SGEVLETTAP GVEEISGLPS
1310 1320 1330 1340 1350
GEVLETTAPG VDEISGLPSG EVLETTAPGV EEISGLPSGE VLETSTSAVG
1360 1370 1380 1390 1400
DLSGLPSGGE VLEISVSGVE DISGLPSGEV VETSASGIED VSELPSGEGL
1410 1420 1430 1440 1450
ETSASGVEDL SRLPSGEEVL EISASGFGDL SGVPSGGEGL ETSASEVGTD
1460 1470 1480 1490 1500
LSGLPSGREG LETSASGAED LSGLPSGKED LVGSASGDLD LGKLPSGTLG
1510 1520 1530 1540 1550
SGQAPETSGL PSGFSGEYSG VDLGSGPPSG LPDFSGLPSG FPTVSLVDST
1560 1570 1580 1590 1600
LVEVVTASTA SELEGRGTIG ISGAGEISGL PSSELDISGR ASGLPSGTEL
1610 1620 1630 1640 1650
SGQASGSPDV SGEIPGLFGV SGQPSGFPDT SGETSGVTEL SGLSSGQPGV
1660 1670 1680 1690 1700
SGEASGVLYG TSQPFGITDL SGETSGVPDL SGQPSGLPGF SGATSGVPDL
1710 1720 1730 1740 1750
VSGTTSGSGE SSGITFVDTS LVEVAPTTFK EEEGLGSVEL SGLPSGEADL
1760 1770 1780 1790 1800
SGKSGMVDVS GQFSGTVDSS GFTSQTPEFS GLPSGIAEVS GESSRAEIGS
1810 1820 1830 1840 1850
SLPSGAYYGS GTPSSFPTVS LVDRTLVESV TQAPTAQEAG EGPSGILELS
1860 1870 1880 1890 1900
GAHSGAPDMS GEHSGFLDLS GLQSGLIEPS GEPPGTPYFS GDFASTTNVS
1910 1920 1930 1940 1950
GESSVAMGTS GEASGLPEVT LITSEFVEGV TEPTISQELG QRPPVTHTPQ
1960 1970 1980 1990 2000
LFESSGKVST AGDISGATPV LPGSGVEVSS VPESSSETSA YPEAGFGASA
2010 2020 2030 2040 2050
APEASREDSG SPDLSETTSA FHEANLERSS GLGVSGSTLT FQEGEASAAP
2060 2070 2080 2090 2100
EVSGESTTTS DVGTEAPGLP SATPTASGDR TEISGDLSGH TSQLGVVIST
2110 2120 2130 2140 2150
SIPESEWTQQ TQRPAETHLE IESSSLLYSG EETHTVETAT SPTDASIPAS
2160 2170 2180 2190 2200
PEWKRESEST AAAPARSCAE EPCGAGTCKE TEGHVICLCP PGYTGEHCNI
2210 2220 2230 2240 2250
DQEVCEEGWN KYQGHCYRHF PDRETWVDAE RRCREQQSHL SSIVTPEEQE
2260 2270 2280 2290 2300
FVNNNAQDYQ WIGLNDRTIE GDFRWSDGHP MQFENWRPNQ PDNFFAAGED
2310 2320 2330 2340 2350
CVVMIWHEKG EWNDVPCNYH LPFTCKKGTV ACGEPPVVEH ARTFGQKKDR
2360 2370 2380 2390 2400
YEINSLVRYQ CTEGFVQRHM PTIRCQPSGH WEEPRITCTD ATTYKRRLQK
2410
RSSRHPRRSR PSTAH
Length:2,415
Mass (Da):250,193
Last modified:August 1, 1992 - v2
Checksum:i1288937E1B98C6B6
GO
Isoform 2 (identifier: P16112-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:2,377
Mass (Da):246,306
Checksum:iCC3F3E0D74B00DAD
GO
Isoform 3 (identifier: P16112-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:2,316
Mass (Da):239,235
Checksum:i44ABD9AF85CC3612
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti766 – 7661E → A in AAC60643. (PubMed:7827755)Curated
Sequence conflicti847 – 8471E → V in AAC60643. (PubMed:7827755)Curated
Sequence conflicti1928 – 19281E → A in CAA35463. (PubMed:8611178)Curated
Sequence conflicti1964 – 19641I → V in CAA35463. (PubMed:8611178)Curated
Sequence conflicti1964 – 19641I → V in AAA35726. (PubMed:2789216)Curated
Sequence conflicti2070 – 20701P → A in AAA35726. (PubMed:2789216)Curated
Sequence conflicti2391 – 23911A → P in CAA35463. (PubMed:8611178)Curated
Sequence conflicti2391 – 23911A → P in AAA35726. (PubMed:2789216)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti102 – 1021D → E.
Corresponds to variant rs16942318 [ dbSNP | Ensembl ].
VAR_056152
Natural varianti275 – 2751R → Q.
Corresponds to variant rs34949187 [ dbSNP | Ensembl ].
VAR_056153
Natural varianti1943 – 19431P → L.
Corresponds to variant rs35061438 [ dbSNP | Ensembl ].
VAR_056154
Natural varianti2005 – 20051S → R.
Corresponds to variant rs34153007 [ dbSNP | Ensembl ].
VAR_056155
Natural varianti2266 – 22661D → N in SEMD-ACAN; creates a functional N-glycosylation site; does not adversely affect protein trafficking and secretion. 1 Publication
VAR_063053
Natural varianti2303 – 23031V → M in OD. 1 Publication
VAR_063765

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2163 – 220038Missing in isoform 2 and isoform 3. 2 PublicationsVSP_003074Add
BLAST
Alternative sequencei2330 – 239061Missing in isoform 3. 1 PublicationVSP_003075Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA39086.
UniGeneiHs.2159.
Hs.616395.

Polymorphism databases

DMDMi129886.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Aggrecan

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi A39086.
UniGenei Hs.2159.
Hs.616395.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4MD4 X-ray 1.95 C 89-103 [» ]
ProteinModelPortali P16112.
SMRi P16112. Positions 31-135, 154-247, 263-349, 479-572, 588-673, 2165-2200, 2203-2369.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P16112. 1 interaction.
STRINGi 9606.ENSP00000268134.

PTM databases

PhosphoSitei P16112.

Polymorphism databases

DMDMi 129886.

Proteomic databases

PaxDbi P16112.
PRIDEi P16112.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

GeneCardsi GC15P089346.
H-InvDB HIX0026812.
HGNCi HGNC:319. ACAN.
HPAi CAB016377.
MIMi 155760. gene.
165800. phenotype.
608361. phenotype.
612813. phenotype.
neXtProti NX_P16112.
Orphaneti 251262. Familial osteochondritis dissecans.
171866. Spondyloepimetaphyseal dysplasia, aggrecan type.
93283. Spondyloepiphyseal dysplasia, Kimberley type.
PharmGKBi PA24616.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000168421.
HOVERGENi HBG007982.
InParanoidi P16112.
PhylomeDBi P16112.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_121120. Keratan sulfate biosynthesis.
REACT_121313. Keratan sulfate degradation.
REACT_163906. ECM proteoglycans.
REACT_267635. Defective B4GALT1 causes B4GALT1-CDG (CDG-2d).
REACT_267713. Defective CHST6 causes MCDC1.

Miscellaneous databases

ChiTaRSi ACAN. human.
PMAP-CutDB P16112.
PROi P16112.
SOURCEi Search...

Gene expression databases

CleanExi HS_ACAN.
Genevestigatori P16112.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
3.10.100.10. 5 hits.
InterProi IPR001304. 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 ]
Pfami PF00008. EGF. 1 hit.
PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 1 hit.
PF07686. V-set. 1 hit.
PF00193. Xlink. 4 hits.
[Graphical view ]
PRINTSi PR01265. LINKMODULE.
SMARTi SM00032. CCP. 1 hit.
SM00034. CLECT. 1 hit.
SM00181. EGF. 1 hit.
SM00409. IG. 1 hit.
SM00445. LINK. 4 hits.
[Graphical view ]
SUPFAMi SSF56436. SSF56436. 5 hits.
SSF57535. SSF57535. 1 hit.
PROSITEi PS00615. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiPGCA_HUMAN
AccessioniPrimary (citable) accession number: P16112
Secondary accession number(s): Q13650
, Q9UCD3, Q9UCP4, Q9UCP5, Q9UDE0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: August 1, 1992
Last modified: November 26, 2014
This is version 169 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 15
    Human chromosome 15: 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

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