P48594 · SPB4_HUMAN

  • Protein
    Serpin B4
  • Gene
    SERPINB4
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

May act as a protease inhibitor to modulate the host immune response against tumor cells.

Features

Showing features for site.

139050100150200250300350
TypeIDPosition(s)Description
Site354-355Reactive bond

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 Componentcytosol
Cellular Componentextracellular space
Cellular Componentplasma membrane
Molecular Functionenzyme binding
Molecular Functionprotease binding
Molecular Functionserine-type endopeptidase inhibitor activity
Biological Processnegative regulation of peptidase activity
Biological Processprotection from natural killer cell mediated cytotoxicity
Biological Processregulation of proteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Serpin B4
  • Alternative names
    • Leupin
    • Peptidase inhibitor 11 (PI-11)
    • Squamous cell carcinoma antigen 2 (SCCA-2)

Gene names

    • Name
      SERPINB4
    • Synonyms
      PI11, SCCA2

Organism names

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

Accessions

  • Primary accession
    P48594
  • Secondary accessions
    • A8K847

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Note: Seems to also be secreted in plasma by cancerous cells but at a low level.

Keywords

Disease & Variants

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 745 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 modified residue, chain.

TypeIDPosition(s)Description
Modified residue1N-acetylmethionine
ChainPRO_00000941041-390Serpin B4

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Squamous cells.

Gene expression databases

Organism-specific databases

Interaction

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P48594HOXD10 P283582EBI-1055490, EBI-12690664
BINARY P48594IL18 Q141162EBI-1055490, EBI-3910835
BINARY P48594SERPINB3 P295085EBI-1055490, EBI-359110

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Sequence similarities

Belongs to the serpin family. Ov-serpin subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    390
  • Mass (Da)
    44,854
  • Last updated
    1996-10-01 v2
  • Checksum
    04E213CD892587D5
MNSLSEANTKFMFDLFQQFRKSKENNIFYSPISITSALGMVLLGAKDNTAQQISKVLHFDQVTENTTEKAATYHVDRSGNVHHQFQKLLTEFNKSTDAYELKIANKLFGEKTYQFLQEYLDAIKKFYQTSVESTDFANAPEESRKKINSWVESQTNEKIKNLFPDGTIGNDTTLVLVNAIYFKGQWENKFKKENTKEEKFWPNKNTYKSVQMMRQYNSFNFALLEDVQAKVLEIPYKGKDLSMIVLLPNEIDGLQKLEEKLTAEKLMEWTSLQNMRETCVDLHLPRFKMEESYDLKDTLRTMGMVNIFNGDADLSGMTWSHGLSVSKVLHKAFVEVTEEGVEAAAATAVVVVELSSPSTNEEFCCNHPFLFFIRQNKTNSILFYGRFSSP

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
C9JZ65C9JZ65_HUMANSERPINB4211
H0Y5H9H0Y5H9_HUMANSERPINB4371

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict353in Ref. 4; BAF84901

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X89015
EMBL· GenBank· DDBJ
CAA61420.1
EMBL· GenBank· DDBJ
mRNA
U19557
EMBL· GenBank· DDBJ
AAA97553.1
EMBL· GenBank· DDBJ
mRNA
U19576
EMBL· GenBank· DDBJ
AAA92602.1
EMBL· GenBank· DDBJ
Genomic DNA
U19570
EMBL· GenBank· DDBJ
AAA92602.1
EMBL· GenBank· DDBJ
Genomic DNA
U19571
EMBL· GenBank· DDBJ
AAA92602.1
EMBL· GenBank· DDBJ
Genomic DNA
U19572
EMBL· GenBank· DDBJ
AAA92602.1
EMBL· GenBank· DDBJ
Genomic DNA
U19574
EMBL· GenBank· DDBJ
AAA92602.1
EMBL· GenBank· DDBJ
Genomic DNA
U19575
EMBL· GenBank· DDBJ
AAA92602.1
EMBL· GenBank· DDBJ
Genomic DNA
AB035089
EMBL· GenBank· DDBJ
BAB21525.1
EMBL· GenBank· DDBJ
Genomic DNA
AK292212
EMBL· GenBank· DDBJ
BAF84901.1
EMBL· GenBank· DDBJ
mRNA
BC017401
EMBL· GenBank· DDBJ
AAH17401.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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