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P04083 (ANXA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 183. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Annexin A1
Alternative name(s):
Annexin I
Annexin-1
Calpactin II
Calpactin-2
Chromobindin-9
Lipocortin I
Phospholipase A2 inhibitory protein
p35
Gene names
Name:ANXA1
Synonyms:ANX1, LPC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. This protein regulates phospholipase A2 activity. It seems to bind from two to four calcium ions with high affinity.

Subunit structure

Homodimer in placenta (20%); linked by transglutamylation. Interacts with DYSF By similarity. Ref.7

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Cell projectioncilium By similarity. Basolateral cell membrane By similarity. Note: Found in the cilium, nucleus and basolateral cell membrane of ciliated cells in the tracheal endothelium By similarity. Found in the cytoplasm of type II pneumocytes and alveolar macrophages By similarity.

Domain

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

Post-translational modification

Phosphorylated by protein kinase C, epidermal growth factor receptor/kinase and TRPM7. Phosphorylation results in loss of the inhibitory activity. Ref.5 Ref.8

Sequence similarities

Belongs to the annexin family.

Contains 4 annexin repeats.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Cilium
Cytoplasm
Membrane
Nucleus
   DomainAnnexin
Repeat
   LigandCalcium
Calcium/phospholipid-binding
   Molecular functionPhospholipase A2 inhibitor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processalpha-beta T cell differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

arachidonic acid secretion

Inferred from electronic annotation. Source: Ensembl

cell surface receptor signaling pathway

Traceable author statement PubMed 10882119. Source: ProtInc

cellular component movement

Traceable author statement PubMed 10882119. Source: ProtInc

cellular response to glucocorticoid stimulus

Inferred from direct assay Ref.1. Source: BHF-UCL

cellular response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

endocrine pancreas development

Inferred from electronic annotation. Source: Ensembl

estrous cycle phase

Inferred from electronic annotation. Source: Ensembl

gliogenesis

Inferred from electronic annotation. Source: Ensembl

hepatocyte differentiation

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Traceable author statement PubMed 10882119. Source: ProtInc

insulin secretion

Inferred from electronic annotation. Source: Ensembl

keratinocyte differentiation

Inferred from direct assay PubMed 10908733. Source: UniProtKB

negative regulation of acute inflammatory response

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Traceable author statement PubMed 16130169. Source: UniProtKB

negative regulation of protein secretion

Inferred from electronic annotation. Source: Ensembl

neutrophil clearance

Inferred from mutant phenotype PubMed 21957127. Source: BHF-UCL

peptide cross-linking

Inferred from direct assay PubMed 10908733. Source: UniProtKB

positive regulation of G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of neutrophil apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of prostaglandin biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of vesicle fusion

Inferred from direct assay PubMed 2138016. Source: UniProtKB

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

response to X-ray

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbasolateral plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cilium

Inferred from electronic annotation. Source: UniProtKB-SubCell

cornified envelope

Inferred from direct assay PubMed 10908733. Source: UniProtKB

cytoplasm

Traceable author statement PubMed 16130169. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 22664934PubMed 23580065. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

mitochondrial membrane

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay. Source: HPA

protein complex

Inferred from electronic annotation. Source: Ensembl

sarcolemma

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium ion binding

Traceable author statement PubMed 2967291. Source: ProtInc

calcium-dependent phospholipid binding

Inferred from direct assay PubMed 2138016. Source: UniProtKB

phospholipase A2 inhibitor activity

Inferred from direct assay PubMed 3013422. Source: UniProtKB

protein binding, bridging

Inferred from direct assay PubMed 10908733. Source: UniProtKB

receptor binding

Traceable author statement PubMed 10882119. Source: ProtInc

structural molecule activity

Inferred from direct assay PubMed 10908733. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IKBKGQ9Y6K96EBI-354007,EBI-81279
RIPK1Q135465EBI-354007,EBI-358507

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 346345Annexin A1
PRO_0000067460

Regions

Repeat51 – 11161Annexin 1
Repeat123 – 18361Annexin 2
Repeat207 – 26761Annexin 3
Repeat282 – 34261Annexin 4

Amino acid modifications

Modified residue21N-acetylalanine Ref.6
Modified residue51Phosphoserine; by TRPM7 Ref.8
Modified residue211Phosphotyrosine; by EGFR Ref.5
Modified residue241Phosphothreonine
Modified residue271Phosphoserine; by PKC Ref.5
Modified residue371Phosphoserine Ref.11
Modified residue581N6-acetyllysine By similarity
Modified residue2391N6-acetyllysine Ref.10
Modified residue3121N6-acetyllysine Ref.10
Cross-link19Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)

Secondary structure

............... 346
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04083 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 14B42E1FA4178EC0

FASTA34638,714
        10         20         30         40         50         60 
MAMVSEFLKQ AWFIENEEQE YVQTVKSSKG GPGSAVSPYP TFNPSSDVAA LHKAIMVKGV 

        70         80         90        100        110        120 
DEATIIDILT KRNNAQRQQI KAAYLQETGK PLDETLKKAL TGHLEEVVLA LLKTPAQFDA 

       130        140        150        160        170        180 
DELRAAMKGL GTDEDTLIEI LASRTNKEIR DINRVYREEL KRDLAKDITS DTSGDFRNAL 

       190        200        210        220        230        240 
LSLAKGDRSE DFGVNEDLAD SDARALYEAG ERRKGTDVNV FNTILTTRSY PQLRRVFQKY 

       250        260        270        280        290        300 
TKYSKHDMNK VLDLELKGDI EKCLTAIVKC ATSKPAFFAE KLHQAMKGVG TRHKALIRIM 

       310        320        330        340 
VSRSEIDMND IKAFYQKMYG ISLCQAILDE TKGDYEKILV ALCGGN 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of human lipocortin, a phospholipase A2 inhibitor with potential anti-inflammatory activity."
Wallner B.P., Mattaliano R.J., Hession C., Cate R.L., Tizard R., Sinclair L.K., Foeller C., Chow E.P., Browning J.L., Ramachandran K.L., Pepinsky R.B.
Nature 320:77-81(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Correlation of gene and protein structure of rat and human lipocortin I."
Kovacic R.T., Tizard R., Cate R.L., Frey A.Z., Wallner B.P.
Biochemistry 30:9015-9021(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Structural characterization of a biologically active human lipocortin 1 expressed in Escherichia coli."
Arcone R., Arpaia G., Ruoppolo M., Malorni A., Pucci P., Marino G., Ialenti A., di Rosa M., Ciliberto G.
Eur. J. Biochem. 211:347-355(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
Tissue: Cervix and Lung.
[5]"Location of sites in human lipocortin I that are phosphorylated by protein tyrosine kinases and protein kinases A and C."
Varticovski L., Chahwala S.B., Whitman M., Cantley L., Schindler D., Chow E.P., Sinclair L.K., Pepinsky R.B.
Biochemistry 27:3682-3690(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION AT TYR-21 BY EGFR AND SER-27 BY PKC.
[6]"Characterization by tandem mass spectrometry of structural modifications in proteins."
Biemann K., Scoble H.A.
Science 237:992-998(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT ALA-2, MASS SPECTROMETRY.
[7]"A dimeric form of lipocortin-1 in human placenta."
Pepinsky R.B., Sinclair L.K., Chow E.P., O'Brine-Greco B.
Biochem. J. 263:97-103(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: DIMERIZATION.
[8]"Phosphorylation of annexin I by TRPM7 channel-kinase."
Dorovkov M.V., Ryazanov A.G.
J. Biol. Chem. 279:50643-50646(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-5 BY TRPM7.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239 AND LYS-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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].
[13]"Crystal structure of human annexin I at 2.5-A resolution."
Weng X., Luecke H., Song I.S., Kang D.S., Kim S.-H., Huber R.
Protein Sci. 2:448-458(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[14]"NMR solution structure of domain 1 of human annexin I shows an autonomous folding unit."
Gao J., Li Y., Yan H.
J. Biol. Chem. 274:2971-2977(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 41-113.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05908 mRNA. Translation: CAA29338.1.
BC001275 mRNA. Translation: AAH01275.1.
BC035993 mRNA. Translation: AAH35993.1.
PIRLUHU. A03080.
RefSeqNP_000691.1. NM_000700.1.
UniGeneHs.494173.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AINX-ray2.50A33-346[»]
1BO9NMR-A41-113[»]
1QLSX-ray2.30D2-12[»]
ProteinModelPortalP04083.
SMRP04083. Positions 2-344.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106798. 51 interactions.
DIPDIP-32875N.
IntActP04083. 38 interactions.
MINTMINT-1212274.
STRING9606.ENSP00000257497.

Chemistry

DrugBankDB00240. Alclometasone.
DB00288. Amcinonide.
DB00394. Beclomethasone.
DB00443. Betamethasone.
DB01013. Clobetasol.
DB00838. Clocortolone.
DB01260. Desonide.
DB00547. Desoximetasone.
DB01234. Dexamethasone.
DB00223. Diflorasone.
DB00663. Flumethasone Pivalate.
DB00596. Halobetasol Propionate.
DB00769. Hydrocortamate.
DB00741. Hydrocortisone.
DB00873. Loteprednol Etabonate.
DB00959. Methylprednisolone.
DB00764. Mometasone.
DB01130. Prednicarbate.
DB00635. Prednisone.
DB00896. Rimexolone.
DB00620. Triamcinolone.

Protein family/group databases

TCDB1.A.31.1.3. the annexin (annexin) family.

PTM databases

PhosphoSiteP04083.

Polymorphism databases

DMDM113944.

2D gel databases

DOSAC-COBS-2DPAGEP04083.
REPRODUCTION-2DPAGEIPI00218918.
P04083.
UCD-2DPAGEP04083.

Proteomic databases

PaxDbP04083.
PeptideAtlasP04083.
PRIDEP04083.

Protocols and materials databases

DNASU301.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257497; ENSP00000257497; ENSG00000135046.
ENST00000376911; ENSP00000366109; ENSG00000135046.
GeneID301.
KEGGhsa:301.
UCSCuc004ajf.1. human.

Organism-specific databases

CTD301.
GeneCardsGC09P075766.
HGNCHGNC:533. ANXA1.
HPACAB013023.
CAB035987.
CAB058693.
HPA011271.
HPA011272.
MIM151690. gene.
neXtProtNX_P04083.
PharmGKBPA24823.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG282829.
HOGENOMHOG000158803.
HOVERGENHBG061815.
InParanoidP04083.
KOK17091.
OMAMNDIKAC.
OrthoDBEOG74XS72.
PhylomeDBP04083.
TreeFamTF105452.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkP04083.

Gene expression databases

ArrayExpressP04083.
BgeeP04083.
CleanExHS_ANXA1.
GenevestigatorP04083.

Family and domain databases

Gene3D1.10.220.10. 4 hits.
InterProIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002388. AnnexinI.
[Graphical view]
PfamPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSPR00196. ANNEXIN.
PR00197. ANNEXINI.
SMARTSM00335. ANX. 4 hits.
[Graphical view]
PROSITEPS00223. ANNEXIN. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSANXA1. human.
EvolutionaryTraceP04083.
GeneWikiAnnexin_A1.
GenomeRNAi301.
NextBio1213.
PROP04083.
SOURCESearch...

Entry information

Entry nameANXA1_HUMAN
AccessionPrimary (citable) accession number: P04083
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 183 of the entry and version 2 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 chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM