P13928 · ANXA8_HUMAN

  • Protein
    Annexin A8
  • Gene
    ANXA8
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade.

Features

Showing features for binding site.

132750100150200250300
TypeIDPosition(s)Description
Binding site266Ca2+ (UniProtKB | ChEBI)
Binding site268Ca2+ (UniProtKB | ChEBI)
Binding site270Ca2+ (UniProtKB | ChEBI)
Binding site310Ca2+ (UniProtKB | ChEBI)

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 Componentcollagen-containing extracellular matrix
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentlate endosome membrane
Cellular Componentplasma membrane
Cellular Componentsarcolemma
Cellular Componentvesicle membrane
Molecular Functionactin filament binding
Molecular Functioncalcium ion binding
Molecular Functioncalcium-dependent phospholipid binding
Molecular Functionphosphatidylinositol-3,4,5-trisphosphate binding
Molecular Functionphosphatidylinositol-3,4-bisphosphate binding
Molecular Functionphosphatidylinositol-4,5-bisphosphate binding
Molecular Functionphosphatidylserine binding
Biological Processblood coagulation
Biological Processendosomal transport
Biological Processendosome organization
Biological Processnegative regulation of phospholipase A2 activity
Biological Processnegative regulation of serine-type endopeptidase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Annexin A8
  • Alternative names
    • Annexin VIII
    • Annexin-8
    • Vascular anticoagulant-beta
      (VAC-beta
      )

Gene names

    • Name
      ANXA8
    • Synonyms
      ANX8

Organism names

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

Accessions

  • Primary accession
    P13928
  • Secondary accessions
    • A6NDE6
    • A6NLM1
    • B4DKI1
    • B4DTC9
    • Q5T2P8

Proteomes

Organism-specific databases

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_0006046in dbSNP:rs3870786
Natural variantVAR_030630177in dbSNP:rs75345346

Variants

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

The viewer provides 273 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).

TypeIDPosition(s)SourceDescription
ChainPRO_00000675031-327UniProtAnnexin A8
Modified residue (large scale data)31PRIDEPhosphotyrosine

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Family & Domains

Features

Showing features for repeat.

TypeIDPosition(s)Description
Repeat21-92Annexin 1
Repeat93-164Annexin 2
Repeat177-249Annexin 3
Repeat253-324Annexin 4

Domain

A pair of annexin repeats may form one binding site for calcium and phospholipid.

Sequence similarities

Belongs to the annexin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

P13928-1

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
    327
  • Mass (Da)
    36,881
  • Last updated
    2008-11-25 v3
  • Checksum
    5DBBDBB6E723C298
MAWWKSWIEQEGVTVKSSSHFNPDPDAETLYKAMKGIGTNEQAIIDVLTKRSNTQRQQIAKSFKAQFGKDLTETLKSELSGKFERLIVALMYPPYRYEAKELHDAMKGLGTKEGVIIEILASRTKNQLREIMKAYEEDYGSSLEEDIQADTSGYLERILVCLLQGSRDDVSSFVDPGLALQDAQDLYAAGEKIRGTDEMKFITILCTRSATHLLRVFEEYEKIANKSIEDSIKSETHGSLEEAMLTVVKCTQNLHSYFAERLYYAMKGAGTRDGTLIRNIVSRSEIDLNLIKCHFKKMYGKTLSSMIMEDTSGDYKNALLSLVGSDP

P13928-2

P13928-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A075B748A0A075B748_HUMANANXA821
A0A075B765A0A075B765_HUMANANXA8276
A0A087WTN9A0A087WTN9_HUMANANXA8365

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0578058-69in isoform 3
Sequence conflict32in Ref. 3; BAG59193 and 4; CAI12203
Sequence conflict58in Ref. 2; AAB46383
Sequence conflict83in Ref. 2; AAB46383
Alternative sequenceVSP_056397138-141in isoform 2
Alternative sequenceVSP_056398142-327in isoform 2
Sequence conflict157in Ref. 2; AAB46383
Sequence conflict313-314in Ref. 2; AAB46383

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X16662
EMBL· GenBank· DDBJ
CAA34650.1
EMBL· GenBank· DDBJ
mRNA
M81844
EMBL· GenBank· DDBJ
AAB46383.1
EMBL· GenBank· DDBJ
mRNA
AK296573
EMBL· GenBank· DDBJ
BAG59193.1
EMBL· GenBank· DDBJ
mRNA
AK300158
EMBL· GenBank· DDBJ
BAG61941.1
EMBL· GenBank· DDBJ
mRNA
AL391137
EMBL· GenBank· DDBJ
CAI12203.1
EMBL· GenBank· DDBJ
Genomic DNA
AL591684
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC004376
EMBL· GenBank· DDBJ
AAH04376.1
EMBL· GenBank· DDBJ
mRNA
BC073755
EMBL· GenBank· DDBJ
AAH73755.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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