O95171 · SCEL_HUMAN
- ProteinSciellin
- GeneSCEL
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids688 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May function in the assembly or regulation of proteins in the cornified envelope. The LIM domain may be involved in homotypic or heterotypic associations and may function to localize sciellin to the cornified envelope.
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 | cornified envelope | |
Cellular Component | cytoplasm | |
Cellular Component | extracellular exosome | |
Cellular Component | perinuclear region of cytoplasm | |
Molecular Function | metal ion binding | |
Biological Process | embryo development ending in birth or egg hatching | |
Biological Process | epidermis development | |
Biological Process | keratinocyte differentiation | |
Biological Process | positive regulation of canonical Wnt signaling pathway | |
Biological Process | response to mechanical stimulus |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSciellin
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO95171
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_047920 | 336 | in dbSNP:rs34164479 | |||
Sequence: V → L | ||||||
Natural variant | VAR_047921 | 386 | in dbSNP:rs2274016 | |||
Sequence: R → K | ||||||
Natural variant | VAR_047922 | 480 | in dbSNP:rs8002725 | |||
Sequence: K → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 824 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 chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000075903 | 1-688 | UniProt | Sciellin | |||
Sequence: MSNVTLRKMSPTGNEMKSTTQGTTRKQQDFHEVNKRRTFLQDNSWIKKRPEEEKDENYGRVVLNRHNSHDALDRKVNERDVPKATISRYSSDDTLDRISDRNDAAKTYKANTLDNQLTNRSMSMFRSLEVTKLQPGGSLNANTSNTIASTSATTPVKKKRQSWFPPPPPGYNASSSTGTRRREPGVHPPIPPKPSSPVSSPNQLRQDNRQIHPPKPGVYTETNRSAERNIRSQDLDNIVKVATSLQRSDKGEELDNLIKMNKSLNRNQGLDSLFRANPKVEEREKRAKSLESLIYMSTRTDKDGKGIQSLGSPIKVNQRTDKNEKGRQNLESVAKVNARMNKTSRRSEDLDNATEVNPKGHENTTGKKDLDGLIKVDPETNKNITRGQSLDNLIKVTPEVKRSNQGSKDLNNFIKVYPGTEKSTEGGQSLDSLIKVTPERNRTNQGNQDLENLIKVIPSANKSSEQGLDEHINVSPKAVKNTDGKQDLDKLIKVNPEIFTNNQRNQDLANLIKVNPAVIRNNQSQDLDNLIKVKPSALRNTNRDQNLENLIEVNSHVSENKNGSSNTGAKQAGPQDTVVYTRTYVENSKSPKDGYQENISGKYIQTVYSTSDRSVIERDMCTYCRKPLGVETKMILDELQICCHSTCFKCEICKQPLENLQAGDSIWIYRQTIHCEPCYSKIMAKWIP | |||||||
Modified residue (large scale data) | 10 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 68 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 83 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 91 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 112 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 196 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 232 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 289 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 289 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 295 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 309 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 312 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 347 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 389 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 389 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 437 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 475 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 524 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 580 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 588 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 590 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 608 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in esophagus. It is also expressed in keratinocytes, amniotic tissue, foreskin stratum spinosum and stratum granulosum, hair follicle and nail.
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O95171 | FXR2 P51116 | 4 | EBI-7543896, EBI-740459 | |
BINARY | O95171 | GOLGA2 Q08379 | 4 | EBI-7543896, EBI-618309 | |
BINARY | O95171 | KIFC3 Q9BVG8 | 3 | EBI-7543896, EBI-2125614 | |
BINARY | O95171 | MTUS2 Q5JR59 | 3 | EBI-7543896, EBI-742948 | |
BINARY | O95171 | NMI Q13287 | 7 | EBI-7543896, EBI-372942 | |
BINARY | O95171 | TSGA10 Q9BZW7 | 3 | EBI-7543896, EBI-744794 | |
BINARY | O95171-2 | NMI Q13287 | 3 | EBI-12056699, EBI-372942 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-27 | Polar residues | ||||
Sequence: MSNVTLRKMSPTGNEMKSTTQGTTRKQ | ||||||
Region | 1-29 | Disordered | ||||
Sequence: MSNVTLRKMSPTGNEMKSTTQGTTRKQQD | ||||||
Compositional bias | 134-158 | Polar residues | ||||
Sequence: QPGGSLNANTSNTIASTSATTPVKK | ||||||
Region | 134-231 | Disordered | ||||
Sequence: QPGGSLNANTSNTIASTSATTPVKKKRQSWFPPPPPGYNASSSTGTRRREPGVHPPIPPKPSSPVSSPNQLRQDNRQIHPPKPGVYTETNRSAERNIR | ||||||
Repeat | 251-266 | 1 | ||||
Sequence: GEELDNLIKMNKSLNR | ||||||
Region | 251-563 | 16 X approximate tandem repeats | ||||
Sequence: GEELDNLIKMNKSLNRNQGLDSLFRANPKVEEREKRAKSLESLIYMSTRTDKDGKGIQSLGSPIKVNQRTDKNEKGRQNLESVAKVNARMNKTSRRSEDLDNATEVNPKGHENTTGKKDLDGLIKVDPETNKNITRGQSLDNLIKVTPEVKRSNQGSKDLNNFIKVYPGTEKSTEGGQSLDSLIKVTPERNRTNQGNQDLENLIKVIPSANKSSEQGLDEHINVSPKAVKNTDGKQDLDKLIKVNPEIFTNNQRNQDLANLIKVNPAVIRNNQSQDLDNLIKVKPSALRNTNRDQNLENLIEVNSHVSENKNG | ||||||
Repeat | 267-286 | 2 | ||||
Sequence: NQGLDSLFRANPKVEEREKR | ||||||
Repeat | 287-306 | 3 | ||||
Sequence: AKSLESLIYMSTRTDKDGKG | ||||||
Repeat | 307-326 | 4 | ||||
Sequence: IQSLGSPIKVNQRTDKNEKG | ||||||
Repeat | 327-346 | 5 | ||||
Sequence: RQNLESVAKVNARMNKTSRR | ||||||
Region | 340-373 | Disordered | ||||
Sequence: MNKTSRRSEDLDNATEVNPKGHENTTGKKDLDGL | ||||||
Compositional bias | 341-373 | Basic and acidic residues | ||||
Sequence: NKTSRRSEDLDNATEVNPKGHENTTGKKDLDGL | ||||||
Repeat | 347-366 | 6 | ||||
Sequence: SEDLDNATEVNPKGHENTTG | ||||||
Repeat | 367-386 | 7 | ||||
Sequence: KKDLDGLIKVDPETNKNITR | ||||||
Repeat | 387-406 | 8 | ||||
Sequence: GQSLDNLIKVTPEVKRSNQG | ||||||
Repeat | 407-426 | 9 | ||||
Sequence: SKDLNNFIKVYPGTEKSTEG | ||||||
Repeat | 427-446 | 10 | ||||
Sequence: GQSLDSLIKVTPERNRTNQG | ||||||
Repeat | 447-465 | 11 | ||||
Sequence: NQDLENLIKVIPSANKSSE | ||||||
Repeat | 466-484 | 12 | ||||
Sequence: QGLDEHINVSPKAVKNTDG | ||||||
Repeat | 485-504 | 13 | ||||
Sequence: KQDLDKLIKVNPEIFTNNQR | ||||||
Repeat | 505-523 | 14 | ||||
Sequence: NQDLANLIKVNPAVIRNNQ | ||||||
Repeat | 524-543 | 15 | ||||
Sequence: SQDLDNLIKVKPSALRNTNR | ||||||
Repeat | 544-563 | 16 | ||||
Sequence: DQNLENLIEVNSHVSENKNG | ||||||
Domain | 619-685 | LIM zinc-binding | ||||
Sequence: DMCTYCRKPLGVETKMILDELQICCHSTCFKCEICKQPLENLQAGDSIWIYRQTIHCEPCYSKIMAK |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
O95171-1
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
- Length688
- Mass (Da)77,552
- Last updated2008-12-16 v2
- ChecksumB97F62DD560B57C3
O95171-2
- Name2
- Differences from canonical
- 231-251: RSQDLDNIVKVATSLQRSDKG → S
O95171-3
- Name3
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F2Z2X8 | F2Z2X8_HUMAN | SCEL | 283 |
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-27 | Polar residues | ||||
Sequence: MSNVTLRKMSPTGNEMKSTTQGTTRKQ | ||||||
Sequence conflict | 37 | in Ref. 2; BAH13533 | ||||
Sequence: R → G | ||||||
Sequence conflict | 124 | in Ref. 6; AAH47536 | ||||
Sequence: M → V | ||||||
Compositional bias | 134-158 | Polar residues | ||||
Sequence: QPGGSLNANTSNTIASTSATTPVKK | ||||||
Alternative sequence | VSP_045288 | 160-181 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 201 | in Ref. 6; AAH47536 | ||||
Sequence: P → T | ||||||
Alternative sequence | VSP_035980 | 231-251 | in isoform 2 | |||
Sequence: RSQDLDNIVKVATSLQRSDKG → S | ||||||
Sequence conflict | 337 | in Ref. 1; AAC78461 | ||||
Sequence: N → D | ||||||
Sequence conflict | 340 | in Ref. 1; AAC78461 | ||||
Sequence: M → T | ||||||
Compositional bias | 341-373 | Basic and acidic residues | ||||
Sequence: NKTSRRSEDLDNATEVNPKGHENTTGKKDLDGL | ||||||
Alternative sequence | VSP_045289 | 367-386 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 680 | in Ref. 3; BAD96440 | ||||
Sequence: S → P |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF045941 EMBL· GenBank· DDBJ | AAC78461.1 EMBL· GenBank· DDBJ | mRNA | ||
AK301659 EMBL· GenBank· DDBJ | BAH13533.1 EMBL· GenBank· DDBJ | mRNA | ||
AK222720 EMBL· GenBank· DDBJ | BAD96440.1 EMBL· GenBank· DDBJ | mRNA | ||
AL137140 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471093 EMBL· GenBank· DDBJ | EAW80568.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471093 EMBL· GenBank· DDBJ | EAW80569.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC047536 EMBL· GenBank· DDBJ | AAH47536.1 EMBL· GenBank· DDBJ | mRNA |