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Protein

Annexin A8

Gene

ANXA8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi266 – 2661Calcium; via carbonyl oxygen
Metal bindingi268 – 2681Calcium; via carbonyl oxygen
Metal bindingi270 – 2701Calcium; via carbonyl oxygen
Metal bindingi310 – 3101Calcium

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • calcium-dependent phospholipid binding Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
  • phosphatidylinositol-3,4-bisphosphate binding Source: UniProtKB
  • phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB

GO - Biological processi

  • blood coagulation Source: UniProtKB-KW
  • endosomal transport Source: UniProtKB
  • endosome organization Source: UniProtKB
  • negative regulation of phospholipase A2 activity Source: UniProtKB
  • negative regulation of serine-type endopeptidase activity Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium, Calcium/phospholipid-binding, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Annexin A8Imported
Alternative name(s):
Annexin VIII1 Publication
Annexin-81 Publication
Vascular anticoagulant-beta1 Publication
Short name:
VAC-beta1 Publication
Gene namesi
Name:ANXA8Imported
Synonyms:ANX8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:546. ANXA8.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • late endosome membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24836.

Polymorphism and mutation databases

BioMutaiANXA8.
DMDMi215274181.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 327327Annexin A8PRO_0000067503Add
BLAST

Proteomic databases

MaxQBiP13928.
PaxDbiP13928.
PRIDEiP13928.

PTM databases

PhosphoSiteiP13928.

Expressioni

Gene expression databases

BgeeiP13928.
CleanExiHS_ANXA8.
ExpressionAtlasiP13928. baseline.
GenevisibleiP13928. HS.

Interactioni

Protein-protein interaction databases

BioGridi575558. 6 interactions.
608549. 8 interactions.
IntActiP13928. 3 interactions.
MINTiMINT-1892975.
STRINGi9606.ENSP00000341674.

Structurei

Secondary structure

1
327
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 3411Combined sources
Beta strandi35 – 384Combined sources
Helixi41 – 488Combined sources
Helixi53 – 6715Combined sources
Helixi71 – 788Combined sources
Helixi81 – 9111Combined sources
Helixi96 – 10712Combined sources
Beta strandi108 – 1103Combined sources
Helixi113 – 12210Combined sources
Helixi125 – 13915Combined sources
Helixi143 – 1508Combined sources
Helixi153 – 16311Combined sources
Beta strandi167 – 1704Combined sources
Helixi176 – 19116Combined sources
Beta strandi193 – 1953Combined sources
Helixi198 – 20710Combined sources
Helixi210 – 22415Combined sources
Helixi228 – 2358Combined sources
Helixi238 – 25215Combined sources
Helixi254 – 26613Combined sources
Beta strandi267 – 2704Combined sources
Helixi273 – 28311Combined sources
Turni284 – 2863Combined sources
Helixi288 – 29912Combined sources
Helixi303 – 3108Combined sources
Helixi313 – 32311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W3WX-ray1.99A1-327[»]
1W45X-ray2.51A/B1-327[»]
ProteinModelPortaliP13928.
SMRiP13928. Positions 8-327.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13928.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati30 – 9061Annexin 1Add
BLAST
Repeati102 – 16261Annexin 2Add
BLAST
Repeati187 – 24761Annexin 3Add
BLAST
Repeati262 – 32261Annexin 4Add
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the annexin family.Curated
Contains 4 annexin repeats.Curated

Keywords - Domaini

Annexin, Repeat

Phylogenomic databases

eggNOGiNOG267770.
GeneTreeiENSGT00760000118972.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP13928.
KOiK17096.
PhylomeDBiP13928.
TreeFamiTF105452.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR009115. AnnexinVIII.
[Graphical view]
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR01808. ANNEXINVIII.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 4 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P13928-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAWWKSWIEQ EGVTVKSSSH FNPDPDAETL YKAMKGIGTN EQAIIDVLTK
60 70 80 90 100
RSNTQRQQIA KSFKAQFGKD LTETLKSELS GKFERLIVAL MYPPYRYEAK
110 120 130 140 150
ELHDAMKGLG TKEGVIIEIL ASRTKNQLRE IMKAYEEDYG SSLEEDIQAD
160 170 180 190 200
TSGYLERILV CLLQGSRDDV SSFVDPGLAL QDAQDLYAAG EKIRGTDEMK
210 220 230 240 250
FITILCTRSA THLLRVFEEY EKIANKSIED SIKSETHGSL EEAMLTVVKC
260 270 280 290 300
TQNLHSYFAE RLYYAMKGAG TRDGTLIRNI VSRSEIDLNL IKCHFKKMYG
310 320
KTLSSMIMED TSGDYKNALL SLVGSDP
Length:327
Mass (Da):36,881
Last modified:November 25, 2008 - v3
Checksum:i5DBBDBB6E723C298
GO
Isoform 2 (identifier: P13928-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     138-141: DYGS → GQQG
     142-327: Missing.

Note: No experimental confirmation available.
Show »
Length:141
Mass (Da):16,070
Checksum:iD7D3F13E09C28D19
GO
Isoform 3 (identifier: P13928-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     8-69: Missing.

Note: No experimental confirmation available.
Show »
Length:265
Mass (Da):30,017
Checksum:iE22DABB4F9AEAE6C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321K → Q in BAG59193 (PubMed:14702039).Curated
Sequence conflicti32 – 321K → Q in CAI12203 (PubMed:15164054).Curated
Sequence conflicti58 – 581Q → T in AAB46383 (PubMed:1313714).Curated
Sequence conflicti83 – 831F → L in AAB46383 (PubMed:1313714).Curated
Sequence conflicti157 – 1571R → S in AAB46383 (PubMed:1313714).Curated
Sequence conflicti313 – 3142GD → RY in AAB46383 (PubMed:1313714).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61S → A.1 Publication
VAR_000604
Natural varianti177 – 1771G → A.2 Publications
Corresponds to variant rs3013886 [ dbSNP | Ensembl ].
VAR_030630

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei8 – 6962Missing in isoform 3. 1 PublicationVSP_057805Add
BLAST
Alternative sequencei138 – 1414DYGS → GQQG in isoform 2. 1 PublicationVSP_056397
Alternative sequencei142 – 327186Missing in isoform 2. 1 PublicationVSP_056398Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16662 mRNA. Translation: CAA34650.1.
M81844 mRNA. Translation: AAB46383.1.
AK296573 mRNA. Translation: BAG59193.1.
AK300158 mRNA. Translation: BAG61941.1.
AL391137 Genomic DNA. Translation: CAI12203.1.
AL591684 Genomic DNA. No translation available.
BC004376 mRNA. Translation: AAH04376.1.
BC073755 mRNA. Translation: AAH73755.1.
CCDSiCCDS73122.1. [P13928-1]
PIRiS06476. LUHU8.
RefSeqiNP_001035173.1. NM_001040084.2. [P13928-1]
NP_001092315.2. NM_001098845.2.
NP_001258631.1. NM_001271702.1.
NP_001258632.1. NM_001271703.1.
UniGeneiHs.535306.
Hs.705389.
Hs.744068.

Genome annotation databases

EnsembliENST00000577813; ENSP00000463244; ENSG00000265190. [P13928-2]
ENST00000585281; ENSP00000462880; ENSG00000265190.
GeneIDi653145.
728113.
KEGGihsa:653145.
hsa:728113.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16662 mRNA. Translation: CAA34650.1.
M81844 mRNA. Translation: AAB46383.1.
AK296573 mRNA. Translation: BAG59193.1.
AK300158 mRNA. Translation: BAG61941.1.
AL391137 Genomic DNA. Translation: CAI12203.1.
AL591684 Genomic DNA. No translation available.
BC004376 mRNA. Translation: AAH04376.1.
BC073755 mRNA. Translation: AAH73755.1.
CCDSiCCDS73122.1. [P13928-1]
PIRiS06476. LUHU8.
RefSeqiNP_001035173.1. NM_001040084.2. [P13928-1]
NP_001092315.2. NM_001098845.2.
NP_001258631.1. NM_001271702.1.
NP_001258632.1. NM_001271703.1.
UniGeneiHs.535306.
Hs.705389.
Hs.744068.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W3WX-ray1.99A1-327[»]
1W45X-ray2.51A/B1-327[»]
ProteinModelPortaliP13928.
SMRiP13928. Positions 8-327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi575558. 6 interactions.
608549. 8 interactions.
IntActiP13928. 3 interactions.
MINTiMINT-1892975.
STRINGi9606.ENSP00000341674.

PTM databases

PhosphoSiteiP13928.

Polymorphism and mutation databases

BioMutaiANXA8.
DMDMi215274181.

Proteomic databases

MaxQBiP13928.
PaxDbiP13928.
PRIDEiP13928.

Protocols and materials databases

DNASUi244.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000577813; ENSP00000463244; ENSG00000265190. [P13928-2]
ENST00000585281; ENSP00000462880; ENSG00000265190.
GeneIDi653145.
728113.
KEGGihsa:653145.
hsa:728113.

Organism-specific databases

CTDi653145.
728113.
GeneCardsiGC10P048255.
HGNCiHGNC:546. ANXA8.
MIMi602396. gene.
neXtProtiNX_P13928.
PharmGKBiPA24836.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG267770.
GeneTreeiENSGT00760000118972.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP13928.
KOiK17096.
PhylomeDBiP13928.
TreeFamiTF105452.

Miscellaneous databases

ChiTaRSiANXA8. human.
EvolutionaryTraceiP13928.
NextBioi35474899.
PROiP13928.
SOURCEiSearch...

Gene expression databases

BgeeiP13928.
CleanExiHS_ANXA8.
ExpressionAtlasiP13928. baseline.
GenevisibleiP13928. HS.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR009115. AnnexinVIII.
[Graphical view]
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR01808. ANNEXINVIII.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1), 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] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Cervix and Placenta.
  4. "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.
    , 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].
  5. "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] (ISOFORM 1), VARIANT ALA-177.
    Tissue: Lung and Pancreas.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS), CALCIUM-BINDING SITES.

Entry informationi

Entry nameiANXA8_HUMAN
AccessioniPrimary (citable) accession number: P13928
Secondary accession number(s): A6NDE6
, A6NLM1, B4DKI1, B4DTC9, Q5T2P8, Q5VTM4, Q6GMY3, Q9BT34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 25, 2008
Last modified: July 22, 2015
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.