Q14515 · SPRL1_HUMAN
- ProteinSPARC-like protein 1
- GeneSPARCL1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids664 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
Features
Showing features for binding site.
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 | collagen-containing extracellular matrix | |
Cellular Component | endoplasmic reticulum lumen | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Cellular Component | glutamatergic synapse | |
Molecular Function | calcium ion binding | |
Molecular Function | collagen binding | |
Molecular Function | extracellular matrix binding | |
Biological Process | signal transduction | |
Biological Process | synaptic membrane adhesion |
Keywords
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSPARC-like protein 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ14515
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_016107 | 49 | in dbSNP:rs13051 | |||
Sequence: A → D | ||||||
Natural variant | VAR_058849 | 106 | in dbSNP:rs1049544 | |||
Sequence: H → D | ||||||
Natural variant | VAR_056578 | 419 | in dbSNP:rs1130643 | |||
Sequence: T → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 842 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue (large scale data), modified residue, disulfide bond.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-16 | UniProt | |||||
Sequence: MKTGLFFLCLLGTAAA | |||||||
Chain | PRO_0000020312 | 17-664 | UniProt | SPARC-like protein 1 | |||
Sequence: IPTNARLLSDHSKPTAETVAPDNTAIPSLRAEAEENEKETAVSTEDDSHHKAEKSSVLKSKEESHEQSAEQGKSSSQELGLKDQEDSDGHLSVNLEYAPTEGTLDIKEDMSEPQEKKLSENTDFLAPGVSSFTDSNQQESITKREENQEQPRNYSHHQLNRSSKHSQGLRDQGNQEQDPNISNGEEEEEKEPGEVGTHNDNQERKTELPREHANSKQEEDNTQSDDILEESDQPTQVSKMQEDEFDQGNQEQEDNSNAEMEEENASNVNKHIQETEWQSQEGKTGLEAISNHKETEEKTVSEALLMEPTDDGNTTPRNHGVDDDGDDDGDDGGTDGPRHSASDDYFIPSQAFLEAERAQSIAYHLKIEEQREKVHENENIGTTEPGEHQEAKKAENSSNEEETSSEGNMRVHAVDSCMSFQCKRGHICKADQQGKPHCVCQDPVTCPPTKPLDQVCGTDNQTYASSCHLFATKCRLEGTKKGHQLQLDYFGACKSIPTCTDFEVIQFPLRMRDWLKNILMQLYEANSEHAGYLNEKQRNKVKKIYLDEKRLLAGDHPIDLLLRDFKKNYHMYVYPVHWQFSELDQHPMDRVLTHSELAPLRASLVPMEHCITRFFEECDPNKDKHITLKEWGHCFGIKEEDIDENLLF | |||||||
Glycosylation | 31 | UniProt | O-linked (GalNAc...) threonine | ||||
Sequence: T | |||||||
Glycosylation | 40 | UniProt | O-linked (GalNAc...) threonine | ||||
Sequence: T | |||||||
Glycosylation | 44 | UniProt | O-linked (GalNAc...) serine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 59 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 76 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 80 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 84 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 84 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 92 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 92 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 116 | UniProt | O-linked (GalNAc...) threonine | ||||
Sequence: T | |||||||
Glycosylation | 169 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue | 171 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 176 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 196 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 198 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 231 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 272 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 280 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 295 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 331 | UniProt | O-linked (GalNAc...) threonine | ||||
Sequence: T | |||||||
Modified residue | 358 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 365 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 398 | UniProt | O-linked (GalNAc...) threonine | ||||
Sequence: T | |||||||
Glycosylation | 412 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 413 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 414 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 420 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 420 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Disulfide bond | 433↔444 | UniProt | |||||
Sequence: CMSFQCKRGHIC | |||||||
Disulfide bond | 438↔454 | UniProt | |||||
Sequence: CKRGHICKADQQGKPHC | |||||||
Disulfide bond | 456↔490 | UniProt | |||||
Sequence: CQDPVTCPPTKPLDQVCGTDNQTYASSCHLFATKC | |||||||
Disulfide bond | 462↔483 | UniProt | |||||
Sequence: CPPTKPLDQVCGTDNQTYASSC | |||||||
Disulfide bond | 472↔509 | UniProt | |||||
Sequence: CGTDNQTYASSCHLFATKCRLEGTKKGHQLQLDYFGAC | |||||||
Glycosylation | 476 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 515↔626 | UniProt | |||||
Sequence: CTDFEVIQFPLRMRDWLKNILMQLYEANSEHAGYLNEKQRNKVKKIYLDEKRLLAGDHPIDLLLRDFKKNYHMYVYPVHWQFSELDQHPMDRVLTHSELAPLRASLVPMEHC | |||||||
Disulfide bond | 634↔650 | UniProt | |||||
Sequence: CDPNKDKHITLKEWGHC |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q14515 | MYOC Q99972 | 2 | EBI-2682673, EBI-11692272 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 25-34 | O-glycosylated at one additional site | ||||
Sequence: SDHSKPTAET | ||||||
Region | 28-360 | Disordered | ||||
Sequence: SKPTAETVAPDNTAIPSLRAEAEENEKETAVSTEDDSHHKAEKSSVLKSKEESHEQSAEQGKSSSQELGLKDQEDSDGHLSVNLEYAPTEGTLDIKEDMSEPQEKKLSENTDFLAPGVSSFTDSNQQESITKREENQEQPRNYSHHQLNRSSKHSQGLRDQGNQEQDPNISNGEEEEEKEPGEVGTHNDNQERKTELPREHANSKQEEDNTQSDDILEESDQPTQVSKMQEDEFDQGNQEQEDNSNAEMEEENASNVNKHIQETEWQSQEGKTGLEAISNHKETEEKTVSEALLMEPTDDGNTTPRNHGVDDDGDDDGDDGGTDGPRHSASDD | ||||||
Compositional bias | 47-85 | Basic and acidic residues | ||||
Sequence: AEAEENEKETAVSTEDDSHHKAEKSSVLKSKEESHEQSA | ||||||
Compositional bias | 118-135 | Basic and acidic residues | ||||
Sequence: GTLDIKEDMSEPQEKKLS | ||||||
Compositional bias | 140-154 | Polar residues | ||||
Sequence: FLAPGVSSFTDSNQQ | ||||||
Compositional bias | 169-196 | Polar residues | ||||
Sequence: NYSHHQLNRSSKHSQGLRDQGNQEQDPN | ||||||
Compositional bias | 207-238 | Basic and acidic residues | ||||
Sequence: EPGEVGTHNDNQERKTELPREHANSKQEEDNT | ||||||
Compositional bias | 244-259 | Polar residues | ||||
Sequence: LEESDQPTQVSKMQED | ||||||
Compositional bias | 286-302 | Polar residues | ||||
Sequence: KHIQETEWQSQEGKTGL | ||||||
Compositional bias | 303-320 | Basic and acidic residues | ||||
Sequence: EAISNHKETEEKTVSEAL | ||||||
Compositional bias | 388-424 | Basic and acidic residues | ||||
Sequence: EKVHENENIGTTEPGEHQEAKKAENSSNEEETSSEGN | ||||||
Region | 388-426 | Disordered | ||||
Sequence: EKVHENENIGTTEPGEHQEAKKAENSSNEEETSSEGNMR | ||||||
Domain | 432-454 | Follistatin-like | ||||
Sequence: SCMSFQCKRGHICKADQQGKPHC | ||||||
Domain | 450-511 | Kazal-like | ||||
Sequence: GKPHCVCQDPVTCPPTKPLDQVCGTDNQTYASSCHLFATKCRLEGTKKGHQLQLDYFGACKS | ||||||
Domain | 622-657 | EF-hand | ||||
Sequence: PMEHCITRFFEECDPNKDKHITLKEWGHCFGIKEED |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q14515-1
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.
- Name1
- Length664
- Mass (Da)75,208
- Last updated2009-09-22 v2
- Checksum0750B0080FDB96B6
Q14515-2
- Name2
- Differences from canonical
- 1-125: Missing
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_056678 | 1-125 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 5 | in Ref. 2; CAA60386 | ||||
Sequence: L → P | ||||||
Sequence conflict | 46 | in Ref. 2; CAA60386 | ||||
Sequence: R → W | ||||||
Compositional bias | 47-85 | Basic and acidic residues | ||||
Sequence: AEAEENEKETAVSTEDDSHHKAEKSSVLKSKEESHEQSA | ||||||
Sequence conflict | 116 | in Ref. 1; CAA57650 | ||||
Sequence: T → S | ||||||
Compositional bias | 118-135 | Basic and acidic residues | ||||
Sequence: GTLDIKEDMSEPQEKKLS | ||||||
Sequence conflict | 127 | in Ref. 2; CAA60386 | ||||
Sequence: S → I | ||||||
Compositional bias | 140-154 | Polar residues | ||||
Sequence: FLAPGVSSFTDSNQQ | ||||||
Compositional bias | 169-196 | Polar residues | ||||
Sequence: NYSHHQLNRSSKHSQGLRDQGNQEQDPN | ||||||
Compositional bias | 207-238 | Basic and acidic residues | ||||
Sequence: EPGEVGTHNDNQERKTELPREHANSKQEEDNT | ||||||
Compositional bias | 244-259 | Polar residues | ||||
Sequence: LEESDQPTQVSKMQED | ||||||
Compositional bias | 286-302 | Polar residues | ||||
Sequence: KHIQETEWQSQEGKTGL | ||||||
Compositional bias | 303-320 | Basic and acidic residues | ||||
Sequence: EAISNHKETEEKTVSEAL | ||||||
Compositional bias | 388-424 | Basic and acidic residues | ||||
Sequence: EKVHENENIGTTEPGEHQEAKKAENSSNEEETSSEGN |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X82157 EMBL· GenBank· DDBJ | CAA57650.1 EMBL· GenBank· DDBJ | mRNA | ||
X86693 EMBL· GenBank· DDBJ | CAA60386.1 EMBL· GenBank· DDBJ | mRNA | ||
AK304494 EMBL· GenBank· DDBJ | BAG65302.1 EMBL· GenBank· DDBJ | mRNA | ||
AC093906 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC112250 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |