A0A5K1VW97 · A0A5K1VW97_HUMAN
- ProteinAggrecan core protein
- GeneACAN
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids2530 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | endomembrane system | |
Cellular Component | extracellular region | |
Molecular Function | calcium ion binding | |
Molecular Function | carbohydrate binding | |
Molecular Function | hyaluronic acid binding | |
Biological Process | cell adhesion |
Keywords
- Ligand
Names & Taxonomy
Protein names
- Recommended nameAggrecan core protein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A5K1VW97
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 3,336 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-16 | |||||
Sequence: MTTLLWVFVTLRVITA | ||||||
Chain | PRO_5029793322 | 17-2530 | Aggrecan core protein | |||
Sequence: AVTVETSDHDNSLSVSIPQPSPLRVLLGTSLTIPCYFIDPMHPVTTAPSTAPLAPRIKWSRVSKEKEVVLLVATEGRVRVNSAYQDKVSLPNYPAIPSDATLEVQSLRSNDSGVYRCEVMHGIEDSEATLEVVVKGIVFHYRAISTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKDEFPGVRTYGIRDTNETYDVYCFAEEMEGEVFYATSPEKFTFQEAANECRRLGARLATTGQLYLAWQAGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRTVYVHANQTGYPDPSSRYDAICYTGEDFVDIPENFFGVGGEEDITVQTVTWPDMELPLPRNITEGEARGSVILTVKPIFEVSPSPLEPEEPFTFAPEIGATAFAEVENETGEATRPWGFPTPGLGPATAFTSEDLVVQVTAVPGQPHLPGGVVFHYRPGPTRYSLTFEEAQQACLRTGAVIASPEQLQAAYEAGYEQCDAGWLRDQTVRYPIVSPRTPCVGDKDSSPGVRTYGVRPSTETYDVYCFVDRLEGEVFFATRLEQFTFQEALEFCESHNATLATTGQLYAAWSRGLDKCYAGWLADGSLRYPIVTPRPACGGDKPGVRTVYLYPNQTGLPDPLSRHHAFCFRGISAVPSPGEEEGGTPTSPSGVEEWIVTQVVPGVAAVPVEEETTAVPSGETTAILEFTTEPENQTEWEPAYTPVGTSPLPGILPTWPPTGAATEESTEGPSATEVPSASEEPSPSEVPFPSEEPSPSEEPFPSVRPFPSVELFPSEEPFPSKEPSPSEEPSASEEPYTPSPPVPSWTELPSSGEESGAPDVSGDFTGSGDVSGHLDFSGQLSGDRASGLPSGDLDSSGLTSTVGSGLPVESGLPSGDEERIEWPSTPTVGELPSGAEILEGSASGVGDLSGLPSGEVLETSASGVGDLSGLPSGEVLETTAPGVEDISGLPSGEVLETTAPGVEDISGLPSGEVLETTAPGVEDISGLPSGEVLETTAPGVEDISGLPSGEVLETTAPGVEDISGLPSGEVLETTAPGVEDISGLPSGEVLETAAPGVEDISGLPSGEVLETAAPGVEDISGLPSGEVLETAAPGVEDISGLPSGEVLETAAPGVEDISGLPSGEVLETAAPGVEDISGLPSGEVLETAAPGVEDISGLPSGEVLETAAPGVEDISGLPSGEVLETAAPGVEDISGLPSGEVLETAAPGVEDISGLPSGEVLETAAPGVEDISGLPSGEVLETAAPGVEDISGLPSGEVLETAAPGVEDISGLPSGEVLETAAPGVEDISGLPSGEVLETAAPGVEDISGLPSGEVLETAAPGVEDISGLPSGEVLETAAPGVEDISGLPSGEVLETTAPGVEEISGLPSGEVLETTAPGVDEISGLPSGEVLETTAPGVEEISGLPSGEVLETSTSAVGDLSGLPSGGEVLEISVSGVEDISGLPSGEVVETSASGIEDVSELPSGEGLETSASGVEDLSRLPSGEEVLEISASGFGDLSGLPSGGEGLETSASEVGTDLSGLPSGREGLETSASGAEDLSGLPSGKEDLVGSASGDLDLGKLPSGTLGSGQAPETSGLPSGFSGEYSGVDLGSGPPSGLPDFSGLPSGFPTVSLVDSTLVEVVTASTASELEGRGTIGISGAGEISGLPSSELDISGRASGLPSGTELSGQASGSPDVSGEIPGLFGVSGQPSGFPDTSGETSGVTELSGLSSGQPGISGEASGVLYGTSQPFGITDLSGETSGVPDLSGQPSGLPGFSGATSGVPDLVSGTTSGSGESSGITFVDTSLVEVAPTTFKEEEGLGSVELSGLPSGEADLSGKSGMVDVSGQFSGTVDSSGFTSQTPEFSGLPSGIAEVSGESSRAEIGSSLPSGAYYGSGTPSSFPTVSLVDRTLVESVTQAPTAQEAGEGPSGILELSGAHSGAPDMSGEHSGFLDLSGLQSGLIEPSGEPPGTPYFSGDFASTTNVSGESSVAMGTSGEASGLPEVTLITSEFVEGVTEPTISQELGQRPPVTHTPQLFESSGKVSTAGDISGATPVLPGSGVEVSSVPESSSETSAYPEAGFGASAAPEASREDSGSPDLSETTSAFHEANLERSSGLGVSGSTLTFQEGEASAAPEVSGESTTTSDVGTEAPGLPSATPTASGDRTEISGDLSGHTSQLGVVISTSIPESEWTQQTQRPAETHLEIESSSLLYSGEETHTVETATSPTDASIPASPEWKRESESTAADIDECLSSPCLNGATCVDAIDSFTCLCLPSYEGDLCEIDQEVCEEGWNKYQGHCYRHFPDRETWVDAERRCREQQSHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPMQFENWRPNQPDNFFAAGEDCVVMIWHEKGEWNDVPCNYHLPFTCKKGTVACGEPPVVEHARTFGQKKDRYEINSLVRYQCTEGFVQRHMPTIRCQPSGHWEEPQITCTDPTTYKRRLQKRSSRHPRRSRPSTAH | ||||||
Disulfide bond | 199↔220 | |||||
Sequence: CDAGWLADQTVRYPIHTPREGC | ||||||
Disulfide bond | 297↔318 | |||||
Sequence: CSAGWLADRSVRYPISKARPNC | ||||||
Disulfide bond | 524↔545 | |||||
Sequence: CDAGWLRDQTVRYPIVSPRTPC | ||||||
Disulfide bond | 622↔643 | |||||
Sequence: CYAGWLADGSLRYPIVTPRPAC | ||||||
Disulfide bond | 2304↔2313 | |||||
Sequence: CLPSYEGDLC | ||||||
Disulfide bond | 2447↔2490 | |||||
Sequence: CGEPPVVEHARTFGQKKDRYEINSLVRYQCTEGFVQRHMPTIRC | ||||||
Disulfide bond | 2476↔2503 | |||||
Sequence: CTEGFVQRHMPTIRCQPSGHWEEPQITC |
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 34-147 | Ig-like | ||||
Sequence: PQPSPLRVLLGTSLTIPCYFIDPMHPVTTAPSTAPLAPRIKWSRVSKEKEVVLLVATEGRVRVNSAYQDKVSLPNYPAIPSDATLEVQSLRSNDSGVYRCEVMHGIEDSEATLE | ||||||
Domain | 153-248 | Link | ||||
Sequence: IVFHYRAISTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKDEFPGVRTYGIRDTNETYDVYCFA | ||||||
Domain | 254-350 | Link | ||||
Sequence: EVFYATSPEKFTFQEAANECRRLGARLATTGQLYLAWQAGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRTVYVHANQTGYPDPSSRYDAICYT | ||||||
Domain | 478-573 | Link | ||||
Sequence: VVFHYRPGPTRYSLTFEEAQQACLRTGAVIASPEQLQAAYEAGYEQCDAGWLRDQTVRYPIVSPRTPCVGDKDSSPGVRTYGVRPSTETYDVYCFV | ||||||
Domain | 579-675 | Link | ||||
Sequence: EVFFATRLEQFTFQEALEFCESHNATLATTGQLYAAWSRGLDKCYAGWLADGSLRYPIVTPRPACGGDKPGVRTVYLYPNQTGLPDPLSRHHAFCFR | ||||||
Region | 734-979 | Disordered | ||||
Sequence: TEPENQTEWEPAYTPVGTSPLPGILPTWPPTGAATEESTEGPSATEVPSASEEPSPSEVPFPSEEPSPSEEPFPSVRPFPSVELFPSEEPFPSKEPSPSEEPSASEEPYTPSPPVPSWTELPSSGEESGAPDVSGDFTGSGDVSGHLDFSGQLSGDRASGLPSGDLDSSGLTSTVGSGLPVESGLPSGDEERIEWPSTPTVGELPSGAEILEGSASGVGDLSGLPSGEVLETSASGVGDLSGLPSG | ||||||
Compositional bias | 765-785 | Polar residues | ||||
Sequence: GAATEESTEGPSATEVPSASE | ||||||
Compositional bias | 792-808 | Pro residues | ||||
Sequence: VPFPSEEPSPSEEPFPS | ||||||
Compositional bias | 898-913 | Polar residues | ||||
Sequence: DLDSSGLTSTVGSGLP | ||||||
Region | 1499-1526 | Disordered | ||||
Sequence: SASGIEDVSELPSGEGLETSASGVEDLS | ||||||
Region | 1543-1649 | Disordered | ||||
Sequence: GDLSGLPSGGEGLETSASEVGTDLSGLPSGREGLETSASGAEDLSGLPSGKEDLVGSASGDLDLGKLPSGTLGSGQAPETSGLPSGFSGEYSGVDLGSGPPSGLPDF | ||||||
Compositional bias | 1615-1629 | Polar residues | ||||
Sequence: GSGQAPETSGLPSGF | ||||||
Region | 1687-1772 | Disordered | ||||
Sequence: SGAGEISGLPSSELDISGRASGLPSGTELSGQASGSPDVSGEIPGLFGVSGQPSGFPDTSGETSGVTELSGLSSGQPGISGEASGV | ||||||
Compositional bias | 1709-1723 | Polar residues | ||||
Sequence: LPSGTELSGQASGSP | ||||||
Compositional bias | 1739-1772 | Polar residues | ||||
Sequence: PSGFPDTSGETSGVTELSGLSSGQPGISGEASGV | ||||||
Region | 1784-1827 | Disordered | ||||
Sequence: DLSGETSGVPDLSGQPSGLPGFSGATSGVPDLVSGTTSGSGESS | ||||||
Compositional bias | 1812-1827 | Polar residues | ||||
Sequence: VPDLVSGTTSGSGESS | ||||||
Region | 1883-1902 | Disordered | ||||
Sequence: DSSGFTSQTPEFSGLPSGIA | ||||||
Region | 1948-1977 | Disordered | ||||
Sequence: APTAQEAGEGPSGILELSGAHSGAPDMSGE | ||||||
Compositional bias | 2048-2077 | Polar residues | ||||
Sequence: PTISQELGQRPPVTHTPQLFESSGKVSTAG | ||||||
Region | 2048-2204 | Disordered | ||||
Sequence: PTISQELGQRPPVTHTPQLFESSGKVSTAGDISGATPVLPGSGVEVSSVPESSSETSAYPEAGFGASAAPEASREDSGSPDLSETTSAFHEANLERSSGLGVSGSTLTFQEGEASAAPEVSGESTTTSDVGTEAPGLPSATPTASGDRTEISGDLSG | ||||||
Compositional bias | 2093-2107 | Polar residues | ||||
Sequence: VSSVPESSSETSAYP | ||||||
Compositional bias | 2126-2159 | Polar residues | ||||
Sequence: SPDLSETTSAFHEANLERSSGLGVSGSTLTFQEG | ||||||
Compositional bias | 2166-2204 | Polar residues | ||||
Sequence: EVSGESTTTSDVGTEAPGLPSATPTASGDRTEISGDLSG | ||||||
Compositional bias | 2248-2262 | Polar residues | ||||
Sequence: THTVETATSPTDASI | ||||||
Region | 2248-2273 | Disordered | ||||
Sequence: THTVETATSPTDASIPASPEWKRESE | ||||||
Domain | 2278-2314 | EGF-like | ||||
Sequence: DIDECLSSPCLNGATCVDAIDSFTCLCLPSYEGDLCE | ||||||
Domain | 2327-2441 | C-type lectin | ||||
Sequence: YQGHCYRHFPDRETWVDAERRCREQQSHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPMQFENWRPNQPDNFFAAGEDCVVMIWHEKGEWNDVPCNYHLPFTCK | ||||||
Domain | 2445-2505 | Sushi | ||||
Sequence: VACGEPPVVEHARTFGQKKDRYEINSLVRYQCTEGFVQRHMPTIRCQPSGHWEEPQITCTD | ||||||
Region | 2510-2530 | Disordered | ||||
Sequence: KRRLQKRSSRHPRRSRPSTAH | ||||||
Compositional bias | 2513-2530 | Basic residues | ||||
Sequence: LQKRSSRHPRRSRPSTAH |
Sequence similarities
Belongs to the aggrecan/versican proteoglycan family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,530
- Mass (Da)261,453
- Last updated2021-04-07 v2
- Checksum2B29977EF3716702
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 765-785 | Polar residues | ||||
Sequence: GAATEESTEGPSATEVPSASE | ||||||
Compositional bias | 792-808 | Pro residues | ||||
Sequence: VPFPSEEPSPSEEPFPS | ||||||
Compositional bias | 898-913 | Polar residues | ||||
Sequence: DLDSSGLTSTVGSGLP | ||||||
Compositional bias | 1615-1629 | Polar residues | ||||
Sequence: GSGQAPETSGLPSGF | ||||||
Compositional bias | 1709-1723 | Polar residues | ||||
Sequence: LPSGTELSGQASGSP | ||||||
Compositional bias | 1739-1772 | Polar residues | ||||
Sequence: PSGFPDTSGETSGVTELSGLSSGQPGISGEASGV | ||||||
Compositional bias | 1812-1827 | Polar residues | ||||
Sequence: VPDLVSGTTSGSGESS | ||||||
Compositional bias | 2048-2077 | Polar residues | ||||
Sequence: PTISQELGQRPPVTHTPQLFESSGKVSTAG | ||||||
Compositional bias | 2093-2107 | Polar residues | ||||
Sequence: VSSVPESSSETSAYP | ||||||
Compositional bias | 2126-2159 | Polar residues | ||||
Sequence: SPDLSETTSAFHEANLERSSGLGVSGSTLTFQEG | ||||||
Compositional bias | 2166-2204 | Polar residues | ||||
Sequence: EVSGESTTTSDVGTEAPGLPSATPTASGDRTEISGDLSG | ||||||
Compositional bias | 2248-2262 | Polar residues | ||||
Sequence: THTVETATSPTDASI | ||||||
Compositional bias | 2513-2530 | Basic residues | ||||
Sequence: LQKRSSRHPRRSRPSTAH |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC103982 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |