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Protein

Aggrecan core protein

Gene

ACAN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi2266Calcium 1By similarity1
Metal bindingi2270Calcium 1By similarity1
Metal bindingi2270Calcium 3By similarity1
Metal bindingi2290Calcium 2By similarity1
Metal bindingi2292Calcium 2By similarity1
Metal bindingi2293Calcium 1By similarity1
Metal bindingi2299Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi2299Calcium 2By similarity1
Metal bindingi2300Calcium 1By similarity1
Metal bindingi2300Calcium 3By similarity1
Metal bindingi2313Calcium 2By similarity1
Metal bindingi2314Calcium 2By similarity1
Metal bindingi2314Calcium 2; via carbonyl oxygenBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Lectin, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000157766-MONOMER.
ReactomeiR-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-2022854. Keratan sulfate biosynthesis.
R-HSA-2022857. Keratan sulfate degradation.
R-HSA-3000178. ECM proteoglycans.
R-HSA-3656225. Defective CHST6 causes MCDC1.
R-HSA-3656243. Defective ST3GAL3 causes MCT12 and EIEE15.
R-HSA-3656244. Defective B4GALT1 causes B4GALT1-CDG (CDG-2d).

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
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:319. ACAN.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Spondyloepiphyseal dysplasia type Kimberley (SEDK)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionSpondyloepiphyseal dysplasias are a heterogeneous group of congenital chondrodysplasias that specifically affect epiphyses and vertebrae. The autosomal dominant SEDK is associated with premature degenerative arthropathy.
See also OMIM:608361
Spondyloepimetaphyseal dysplasia aggrecan type (SEMD-ACAN)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:612813
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0630532266D → N in SEMD-ACAN; creates a functional N-glycosylation site; does not adversely affect protein trafficking and secretion. 1 Publication1
Osteochondritis dissecans short stature and early-onset osteoarthritis (OD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:165800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0637652303V → M in OD. 1 Publication1

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

DisGeNETi176.
MalaCardsiACAN.
MIMi165800. phenotype.
608361. phenotype.
612813. phenotype.
Orphaneti251262. Familial osteochondritis dissecans.
171866. Spondyloepimetaphyseal dysplasia, aggrecan type.
93283. Spondyloepiphyseal dysplasia, Kimberley type.
PharmGKBiPA24616.

Polymorphism and mutation databases

DMDMi129886.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 161 PublicationAdd BLAST16
ChainiPRO_000001750517 – 2415Aggrecan core proteinAdd BLAST2399
ChainiPRO_0000017506393 – 2415Aggrecan core protein 2Add BLAST2023

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi51 ↔ 133By similarity
Glycosylationi126N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi175 ↔ 246By similarity
Disulfide bondi199 ↔ 220By similarity
Glycosylationi239N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi273 ↔ 348By similarity
Disulfide bondi297 ↔ 318By similarity
Glycosylationi333N-linked (GlcNAc...)Sequence analysis1
Glycosylationi371O-linked (Xyl...) (keratan sulfate)1 Publication1
Glycosylationi376O-linked (Xyl...) (keratan sulfate)1 Publication1
Glycosylationi387N-linked (GlcNAc...)Sequence analysis1
Glycosylationi434N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi500 ↔ 571By similarity
Disulfide bondi524 ↔ 545By similarity
Disulfide bondi598 ↔ 672By similarity
Glycosylationi602N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi621 ↔ 642By similarity
Glycosylationi657N-linked (GlcNAc...)1 Publication1
Glycosylationi737N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1898N-linked (GlcNAc...)Sequence analysis1
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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei392 – 393Cleavage; by aggrecanase2

Keywords - PTMi

Disulfide bond, Glycoprotein, Proteoglycan

Proteomic databases

PeptideAtlasiP16112.
PRIDEiP16112.

PTM databases

iPTMnetiP16112.
PhosphoSitePlusiP16112.

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.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP16112. 1 interactor.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4MD4X-ray1.95C89-103[»]
ProteinModelPortaliP16112.
SMRiP16112.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 147Ig-like V-typeAdd BLAST114
Domaini153 – 248Link 1PROSITE-ProRule annotationAdd BLAST96
Domaini254 – 350Link 2PROSITE-ProRule annotationAdd BLAST97
Domaini478 – 573Link 3PROSITE-ProRule annotationAdd BLAST96
Domaini579 – 674Link 4PROSITE-ProRule annotationAdd BLAST96
Repeati772 – 7771-16
Repeati778 – 7831-26
Repeati784 – 7891-36
Repeati790 – 7951-46
Repeati796 – 8011-56
Repeati802 – 8071-66
Repeati808 – 8131-7; approximate6
Repeati814 – 8191-8; approximate6
Repeati820 – 8251-96
Repeati826 – 8311-10; approximate6
Repeati832 – 8371-116
Repeati838 – 8431-126
Repeati941 – 9592-1Add BLAST19
Repeati960 – 9782-2Add BLAST19
Repeati979 – 9972-3Add BLAST19
Repeati998 – 10162-4Add BLAST19
Repeati1017 – 10352-5Add BLAST19
Repeati1036 – 10542-6Add BLAST19
Repeati1055 – 10732-7Add BLAST19
Repeati1074 – 10922-8Add BLAST19
Repeati1093 – 11112-9Add BLAST19
Repeati1112 – 11302-10Add BLAST19
Repeati1131 – 11492-11Add BLAST19
Repeati1150 – 11682-12Add BLAST19
Repeati1169 – 11872-13Add BLAST19
Repeati1188 – 12062-14Add BLAST19
Repeati1207 – 12252-15Add BLAST19
Repeati1226 – 12442-16Add BLAST19
Repeati1245 – 12632-17Add BLAST19
Repeati1264 – 12822-18Add BLAST19
Repeati1283 – 13012-19Add BLAST19
Repeati1302 – 13202-20Add BLAST19
Repeati1321 – 13392-21Add BLAST19
Repeati1340 – 13582-22Add BLAST19
Repeati1360 – 13782-23Add BLAST19
Repeati1379 – 13972-24Add BLAST19
Repeati1398 – 14162-25Add BLAST19
Repeati1418 – 14362-26Add BLAST19
Repeati1439 – 14572-27; approximateAdd BLAST19
Repeati1459 – 14772-28Add BLAST19
Repeati1479 – 14972-29Add BLAST19
Domaini2164 – 2199EGF-likePROSITE-ProRule annotationAdd BLAST36
Domaini2201 – 2327C-type lectinPROSITE-ProRule annotationAdd BLAST127
Domaini2330 – 2390SushiPROSITE-ProRule annotationAdd BLAST61

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni48 – 141G1-AAdd BLAST94
Regioni152 – 247G1-BAdd BLAST96
Regioni253 – 349G1-B'Add BLAST97
Regioni477 – 571G2-BAdd BLAST95
Regioni578 – 672G2-B'Add BLAST95
Regioni676 – 848KSAdd BLAST173
Regioni772 – 84312 X 6 AA approximate tandem repeats of E-[GVE]-P-[SFY]-[APT]-[TSP]Add BLAST72
Regioni851 – 1497CS-1Add BLAST647
Regioni941 – 149729 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 BLAST557
Regioni1498 – 2162CS-2Add BLAST665
Regioni2163 – 2415G3Add BLAST253

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

HOGENOMiHOG000168421.
HOVERGENiHBG007982.
InParanoidiP16112.
PhylomeDBiP16112.

Family and domain databases

CDDicd00033. CCP. 1 hit.
Gene3Di2.60.40.10. 1 hit.
3.10.100.10. 5 hits.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR018378. C-type_lectin_CS.
IPR016187. CTDL_fold.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR000538. Link_dom.
IPR000436. Sushi_SCR_CCP_dom.
[Graphical view]
PfamiPF00059. 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.
SM00406. IGv. 1 hit.
SM00445. LINK. 4 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF56436. 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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti766E → A in AAC60643 (PubMed:7827755).Curated1
Sequence conflicti847E → V in AAC60643 (PubMed:7827755).Curated1
Sequence conflicti1928E → A in CAA35463 (PubMed:8611178).Curated1
Sequence conflicti1964I → V in CAA35463 (PubMed:8611178).Curated1
Sequence conflicti1964I → V in AAA35726 (PubMed:2789216).Curated1
Sequence conflicti2070P → A in AAA35726 (PubMed:2789216).Curated1
Sequence conflicti2391A → P in CAA35463 (PubMed:8611178).Curated1
Sequence conflicti2391A → P in AAA35726 (PubMed:2789216).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_056152102D → E.Corresponds to variant rs16942318dbSNPEnsembl.1
Natural variantiVAR_056153275R → Q.Corresponds to variant rs34949187dbSNPEnsembl.1
Natural variantiVAR_0561541943P → L.Corresponds to variant rs35061438dbSNPEnsembl.1
Natural variantiVAR_0561552005S → R.Corresponds to variant rs34153007dbSNPEnsembl.1
Natural variantiVAR_0630532266D → N in SEMD-ACAN; creates a functional N-glycosylation site; does not adversely affect protein trafficking and secretion. 1 Publication1
Natural variantiVAR_0637652303V → M in OD. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0030742163 – 2200Missing in isoform 2 and isoform 3. 2 PublicationsAdd BLAST38
Alternative sequenceiVSP_0030752330 – 2390Missing in isoform 3. 1 PublicationAdd BLAST61

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.

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.
PIRiA39086.
UniGeneiHs.2159.
Hs.616395.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4MD4X-ray1.95C89-103[»]
ProteinModelPortaliP16112.
SMRiP16112.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP16112. 1 interactor.

PTM databases

iPTMnetiP16112.
PhosphoSitePlusiP16112.

Polymorphism and mutation databases

DMDMi129886.

Proteomic databases

PeptideAtlasiP16112.
PRIDEiP16112.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

DisGeNETi176.
GeneCardsiACAN.
H-InvDBHIX0026812.
HGNCiHGNC:319. ACAN.
MalaCardsiACAN.
MIMi155760. gene.
165800. phenotype.
608361. phenotype.
612813. phenotype.
neXtProtiNX_P16112.
Orphaneti251262. Familial osteochondritis dissecans.
171866. Spondyloepimetaphyseal dysplasia, aggrecan type.
93283. Spondyloepiphyseal dysplasia, Kimberley type.
PharmGKBiPA24616.
GenAtlasiSearch...

Phylogenomic databases

HOGENOMiHOG000168421.
HOVERGENiHBG007982.
InParanoidiP16112.
PhylomeDBiP16112.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000157766-MONOMER.
ReactomeiR-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-2022854. Keratan sulfate biosynthesis.
R-HSA-2022857. Keratan sulfate degradation.
R-HSA-3000178. ECM proteoglycans.
R-HSA-3656225. Defective CHST6 causes MCDC1.
R-HSA-3656243. Defective ST3GAL3 causes MCT12 and EIEE15.
R-HSA-3656244. Defective B4GALT1 causes B4GALT1-CDG (CDG-2d).

Miscellaneous databases

ChiTaRSiACAN. human.
PMAP-CutDBP16112.
PROiP16112.
SOURCEiSearch...

Gene expression databases

CleanExiHS_ACAN.

Family and domain databases

CDDicd00033. CCP. 1 hit.
Gene3Di2.60.40.10. 1 hit.
3.10.100.10. 5 hits.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR018378. C-type_lectin_CS.
IPR016187. CTDL_fold.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR000538. Link_dom.
IPR000436. Sushi_SCR_CCP_dom.
[Graphical view]
PfamiPF00059. 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.
SM00406. IGv. 1 hit.
SM00445. LINK. 4 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF56436. 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]
ProtoNetiSearch...

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 30, 2016
This is version 187 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.