O95171 · SCEL_HUMAN

  • Protein
    Sciellin
  • Gene
    SCEL
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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 annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcornified envelope
Cellular Componentcytoplasm
Cellular Componentextracellular exosome
Cellular Componentperinuclear region of cytoplasm
Molecular Functionmetal ion binding
Biological Processembryo development ending in birth or egg hatching
Biological Processepidermis development
Biological Processkeratinocyte differentiation
Biological Processpositive regulation of canonical Wnt signaling pathway
Biological Processresponse to mechanical stimulus

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Sciellin

Gene names

    • Name
      SCEL

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    O95171
  • Secondary accessions
    • B7Z797
    • F5H651
    • Q53H61
    • Q5W0S8
    • Q5W0S9
    • Q86X00

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_047920336in dbSNP:rs34164479
Natural variantVAR_047921386in dbSNP:rs2274016
Natural variantVAR_047922480in dbSNP:rs8002725

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.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data), modified residue.

TypeIDPosition(s)SourceDescription
ChainPRO_00000759031-688UniProtSciellin
Modified residue (large scale data)10PRIDEPhosphoserine
Modified residue (large scale data)68PRIDEPhosphoserine
Modified residue83UniProtN6-acetyllysine
Modified residue (large scale data)91PRIDEPhosphoserine
Modified residue (large scale data)112PRIDEPhosphothreonine
Modified residue (large scale data)196PRIDEPhosphoserine
Modified residue (large scale data)232PRIDEPhosphoserine
Modified residue289UniProtPhosphoserine
Modified residue (large scale data)289PRIDEPhosphoserine
Modified residue (large scale data)295PRIDEPhosphotyrosine
Modified residue (large scale data)309PRIDEPhosphoserine
Modified residue (large scale data)312PRIDEPhosphoserine
Modified residue (large scale data)347PRIDEPhosphoserine
Modified residue389UniProtPhosphoserine
Modified residue (large scale data)389PRIDEPhosphoserine
Modified residue (large scale data)437PRIDEPhosphothreonine
Modified residue (large scale data)475PRIDEPhosphoserine
Modified residue (large scale data)524PRIDEPhosphoserine
Modified residue (large scale data)580PRIDEPhosphotyrosine
Modified residue (large scale data)588PRIDEPhosphoserine
Modified residue (large scale data)590PRIDEPhosphoserine
Modified residue (large scale data)608PRIDEPhosphotyrosine

Keywords

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

Family & Domains

Features

Showing features for compositional bias, region, repeat, domain.

TypeIDPosition(s)Description
Compositional bias1-27Polar residues
Region1-29Disordered
Compositional bias134-158Polar residues
Region134-231Disordered
Repeat251-2661
Region251-56316 X approximate tandem repeats
Repeat267-2862
Repeat287-3063
Repeat307-3264
Repeat327-3465
Region340-373Disordered
Compositional bias341-373Basic and acidic residues
Repeat347-3666
Repeat367-3867
Repeat387-4068
Repeat407-4269
Repeat427-44610
Repeat447-46511
Repeat466-48412
Repeat485-50413
Repeat505-52314
Repeat524-54315
Repeat544-56316
Domain619-685LIM zinc-binding

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

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.

  • Length
    688
  • Mass (Da)
    77,552
  • Last updated
    2008-12-16 v2
  • Checksum
    B97F62DD560B57C3
MSNVTLRKMSPTGNEMKSTTQGTTRKQQDFHEVNKRRTFLQDNSWIKKRPEEEKDENYGRVVLNRHNSHDALDRKVNERDVPKATISRYSSDDTLDRISDRNDAAKTYKANTLDNQLTNRSMSMFRSLEVTKLQPGGSLNANTSNTIASTSATTPVKKKRQSWFPPPPPGYNASSSTGTRRREPGVHPPIPPKPSSPVSSPNQLRQDNRQIHPPKPGVYTETNRSAERNIRSQDLDNIVKVATSLQRSDKGEELDNLIKMNKSLNRNQGLDSLFRANPKVEEREKRAKSLESLIYMSTRTDKDGKGIQSLGSPIKVNQRTDKNEKGRQNLESVAKVNARMNKTSRRSEDLDNATEVNPKGHENTTGKKDLDGLIKVDPETNKNITRGQSLDNLIKVTPEVKRSNQGSKDLNNFIKVYPGTEKSTEGGQSLDSLIKVTPERNRTNQGNQDLENLIKVIPSANKSSEQGLDEHINVSPKAVKNTDGKQDLDKLIKVNPEIFTNNQRNQDLANLIKVNPAVIRNNQSQDLDNLIKVKPSALRNTNRDQNLENLIEVNSHVSENKNGSSNTGAKQAGPQDTVVYTRTYVENSKSPKDGYQENISGKYIQTVYSTSDRSVIERDMCTYCRKPLGVETKMILDELQICCHSTCFKCEICKQPLENLQAGDSIWIYRQTIHCEPCYSKIMAKWIP

O95171-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 231-251: RSQDLDNIVKVATSLQRSDKG → S

O95171-3

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
F2Z2X8F2Z2X8_HUMANSCEL283

Features

Showing features for compositional bias, sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Compositional bias1-27Polar residues
Sequence conflict37in Ref. 2; BAH13533
Sequence conflict124in Ref. 6; AAH47536
Compositional bias134-158Polar residues
Alternative sequenceVSP_045288160-181in isoform 3
Sequence conflict201in Ref. 6; AAH47536
Alternative sequenceVSP_035980231-251in isoform 2
Sequence conflict337in Ref. 1; AAC78461
Sequence conflict340in Ref. 1; AAC78461
Compositional bias341-373Basic and acidic residues
Alternative sequenceVSP_045289367-386in isoform 3
Sequence conflict680in Ref. 3; BAD96440

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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