Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P13928 (ANXA8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Annexin A8
Alternative name(s):
Annexin VIII
Annexin-8
Vascular anticoagulant-beta
Short name=VAC-beta
Gene names
Name:ANXA8
Synonyms:ANX8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Domain

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

Sequence similarities

Belongs to the annexin family.

Contains 4 annexin repeats.

Ontologies

Keywords
   Biological processBlood coagulation
Hemostasis
   Coding sequence diversityPolymorphism
   DomainAnnexin
Repeat
   LigandCalcium
Calcium/phospholipid-binding
Metal-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Inferred from electronic annotation. Source: UniProtKB-KW

endosomal transport

Inferred from mutant phenotype PubMed 18923148. Source: UniProt

endosome organization

Inferred from mutant phenotype PubMed 18923148. Source: UniProt

negative regulation of phospholipase A2 activity

Inferred from direct assay Ref.1. Source: UniProt

negative regulation of serine-type endopeptidase activity

Inferred from direct assay Ref.1. Source: UniProt

   Cellular_componentcytosol

Inferred from direct assay PubMed 18923148. Source: UniProt

late endosome membrane

Inferred from direct assay PubMed 18923148. Source: UniProt

plasma membrane

Inferred from direct assay PubMed 18923148. Source: UniProt

   Molecular_functionactin filament binding

Inferred from direct assay PubMed 16638567. Source: UniProt

calcium ion binding

Inferred from direct assay Ref.6. Source: UniProt

calcium-dependent phospholipid binding

Inferred from direct assay PubMed 16638567Ref.1. Source: UniProt

phosphatidylinositol-3,4,5-trisphosphate binding

Inferred from direct assay PubMed 16638567. Source: UniProt

phosphatidylinositol-3,4-bisphosphate binding

Inferred from direct assay PubMed 16638567. Source: UniProt

phosphatidylinositol-4,5-bisphosphate binding

Inferred from direct assay PubMed 16638567. Source: UniProt

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 327327Annexin A8
PRO_0000067503

Regions

Repeat30 – 9061Annexin 1
Repeat102 – 16261Annexin 2
Repeat187 – 24761Annexin 3
Repeat262 – 32261Annexin 4

Sites

Metal binding2661Calcium; via carbonyl oxygen
Metal binding2681Calcium; via carbonyl oxygen
Metal binding2701Calcium; via carbonyl oxygen
Metal binding3101Calcium

Natural variations

Natural variant61S → A. Ref.1
VAR_000604
Natural variant1771G → A. Ref.1 Ref.4
Corresponds to variant rs3013886 [ dbSNP | Ensembl ].
VAR_030630

Experimental info

Sequence conflict581Q → T in AAB46383. Ref.2
Sequence conflict831F → L in AAB46383. Ref.2
Sequence conflict1571R → S in AAB46383. Ref.2
Sequence conflict313 – 3142GD → RY in AAB46383. Ref.2

Secondary structure

................................................. 327
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13928 [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: 5DBBDBB6E723C298

FASTA32736,881
        10         20         30         40         50         60 
MAWWKSWIEQ EGVTVKSSSH FNPDPDAETL YKAMKGIGTN EQAIIDVLTK RSNTQRQQIA 

        70         80         90        100        110        120 
KSFKAQFGKD LTETLKSELS GKFERLIVAL MYPPYRYEAK ELHDAMKGLG TKEGVIIEIL 

       130        140        150        160        170        180 
ASRTKNQLRE IMKAYEEDYG SSLEEDIQAD TSGYLERILV CLLQGSRDDV SSFVDPGLAL 

       190        200        210        220        230        240 
QDAQDLYAAG EKIRGTDEMK FITILCTRSA THLLRVFEEY EKIANKSIED SIKSETHGSL 

       250        260        270        280        290        300 
EEAMLTVVKC TQNLHSYFAE RLYYAMKGAG TRDGTLIRNI VSRSEIDLNL IKCHFKKMYG 

       310        320 
KTLSSMIMED TSGDYKNALL SLVGSDP 

« Hide

References

« Hide 'large scale' references
[1]"Vascular anticoagulant beta: a novel human Ca2+/phospholipid binding protein that inhibits coagulation and phospholipase A2 activity. Its molecular cloning, expression and comparison with VAC-alpha."
Hauptmann R., Maurer-Fogy I., Krystek E., Bodo G., Andree H., Reutelingsperger C.P.M.
Eur. J. Biochem. 185:63-71(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-6 AND ALA-177.
Tissue: Placenta.
[2]"Specific expression of the annexin VIII gene in acute promyelocytic leukemia."
Chang K.S., Wang G., Freireich E.J., Daly M., Naylor S.L., Trujillo J.M., Stass S.A.
Blood 79:1802-1810(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-177.
Tissue: Lung and Pancreas.
[5]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"The crystal structure of annexin A8 is similar to that of annexin A3."
Rety S., Sopkova-de Oliveira Santos J., Dreyfuss L., Blondeau K., Hofbauerova K., Raguenes-Nicol C., Kerboeuf D., Renouard M., Russo-Marie F., Lewit-Bentley A.
J. Mol. Biol. 345:1131-1139(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS), CALCIUM-BINDING SITES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16662 mRNA. Translation: CAA34650.1.
M81844 mRNA. Translation: AAB46383.1.
AL591684 Genomic DNA. Translation: CAH72203.1.
BC004376 mRNA. Translation: AAH04376.1.
BC073755 mRNA. Translation: AAH73755.1.
PIRLUHU8. S06476.
RefSeqNP_001035173.1. NM_001040084.2.
NP_001092315.2. NM_001098845.2.
NP_001258631.1. NM_001271702.1.
NP_001258632.1. NM_001271703.1.
NP_001621.2. NM_001630.2.
UniGeneHs.535306.
Hs.705389.
Hs.744068.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W3WX-ray1.99A1-327[»]
1W45X-ray2.51A/B1-327[»]
ProteinModelPortalP13928.
SMRP13928. Positions 8-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106745. 7 interactions.
575558. 3 interactions.
IntActP13928. 3 interactions.
MINTMINT-1892975.
STRING9606.ENSP00000341674.

PTM databases

PhosphoSiteP13928.

Polymorphism databases

DMDM215274181.

Proteomic databases

PaxDbP13928.
PRIDEP13928.

Protocols and materials databases

DNASU244.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344416; ENSP00000341674; ENSG00000165390.
ENST00000585281; ENSP00000462880; ENSG00000265190.
GeneID244.
653145.
728113.
KEGGhsa:244.
hsa:653145.
hsa:728113.

Organism-specific databases

CTD244.
653145.
728113.
GeneCardsGC10P048255.
HGNCHGNC:546. ANXA8.
MIM602396. gene.
neXtProtNX_P13928.
PharmGKBPA24836.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG267770.
HOGENOMHOG000158803.
HOVERGENHBG061815.
InParanoidP13928.
KOK17096.
OMAPHFNPDP.
PhylomeDBP13928.
TreeFamTF105452.

Gene expression databases

BgeeP13928.
CleanExHS_ANXA8.
GenevestigatorP13928.

Family and domain databases

Gene3D1.10.220.10. 4 hits.
InterProIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR009115. AnnexinVIII.
[Graphical view]
PfamPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSPR00196. ANNEXIN.
PR01808. ANNEXINVIII.
SMARTSM00335. ANX. 4 hits.
[Graphical view]
PROSITEPS00223. ANNEXIN. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP13928.
GeneWikiANXA8L2.
NextBio972.
PROP13928.
SOURCESearch...

Entry information

Entry nameANXA8_HUMAN
AccessionPrimary (citable) accession number: P13928
Secondary accession number(s): A6NLM1 expand/collapse secondary AC list , Q5VTM4, Q6GMY3, Q9BT34
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM