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Protein

Annexin A1

Gene

ANXA1

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

Functioni

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.

GO - Molecular functioni

  • annealing helicase activity Source: Ensembl
  • calcium-dependent phospholipid binding Source: UniProtKB
  • calcium-dependent protein binding Source: AgBase
  • calcium ion binding Source: ProtInc
  • double-stranded DNA-dependent ATPase activity Source: Ensembl
  • helicase activity Source: Ensembl
  • phospholipase A2 inhibitor activity Source: UniProtKB
  • phospholipid binding Source: ProtInc
  • protein binding, bridging Source: UniProtKB
  • receptor binding Source: ProtInc
  • single-stranded DNA binding Source: Ensembl
  • single-stranded RNA binding Source: Ensembl
  • structural molecule activity Source: UniProtKB

GO - Biological processi

  • alpha-beta T cell differentiation Source: BHF-UCL
  • arachidonic acid secretion Source: Ensembl
  • cell surface receptor signaling pathway Source: ProtInc
  • cellular response to glucocorticoid stimulus Source: BHF-UCL
  • cellular response to hydrogen peroxide Source: Ensembl
  • DNA duplex unwinding Source: Ensembl
  • DNA rewinding Source: Ensembl
  • endocrine pancreas development Source: Ensembl
  • gliogenesis Source: Ensembl
  • hepatocyte differentiation Source: Ensembl
  • inflammatory response Source: ProtInc
  • insulin secretion Source: Ensembl
  • keratinocyte differentiation Source: UniProtKB
  • movement of cell or subcellular component Source: ProtInc
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of interleukin-8 secretion Source: BHF-UCL
  • negative regulation of phospholipase A2 activity Source: Ensembl
  • neutrophil clearance Source: BHF-UCL
  • neutrophil homeostasis Source: BHF-UCL
  • peptide cross-linking Source: UniProtKB
  • positive regulation of G1/S transition of mitotic cell cycle Source: Ensembl
  • positive regulation of neutrophil apoptotic process Source: Ensembl
  • positive regulation of prostaglandin biosynthetic process Source: Ensembl
  • positive regulation of vesicle fusion Source: UniProtKB
  • prolactin secretion Source: Ensembl
  • prostate gland development Source: Ensembl
  • regulation of cell proliferation Source: Ensembl
  • response to drug Source: Ensembl
  • response to estradiol Source: Ensembl
  • response to interleukin-1 Source: Ensembl
  • response to peptide hormone Source: Ensembl
  • response to X-ray Source: Ensembl
  • signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Phospholipase A2 inhibitor

Keywords - Ligandi

Calcium, Calcium/phospholipid-binding

Enzyme and pathway databases

ReactomeiREACT_17044. Muscle contraction.
REACT_18283. G alpha (q) signalling events.
REACT_19231. G alpha (i) signalling events.
REACT_21264. Formyl peptide receptors bind formyl peptides and many other ligands.
SignaLinkiP04083.

Protein family/group databases

TCDBi1.A.31.1.3. the annexin (annexin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Annexin A1
Alternative name(s):
Annexin I
Annexin-1
Calpactin II
Calpactin-2
Chromobindin-9
Lipocortin I
Phospholipase A2 inhibitory protein
p35
Gene namesi
Name:ANXA1
Synonyms:ANX1, LPC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:533. ANXA1.

Subcellular locationi

  • 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. Found in the cytoplasm of type II pneumocytes and alveolar macrophages.By similarity

GO - Cellular componenti

  • basolateral plasma membrane Source: UniProtKB-SubCell
  • cell surface Source: BHF-UCL
  • cilium Source: UniProtKB-SubCell
  • cornified envelope Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • endosome Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • mast cell granule Source: Ensembl
  • mitochondrial membrane Source: Ensembl
  • nucleus Source: BHF-UCL
  • plasma membrane Source: HPA
  • protein complex Source: Ensembl
  • sarcolemma Source: Ensembl
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24823.

Chemistry

DrugBankiDB00288. Amcinonide.
DB01234. Dexamethasone.
DB00741. Hydrocortisone.

Polymorphism and mutation databases

BioMutaiANXA1.
DMDMi113944.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 346345Annexin A1PRO_0000067460Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei5 – 51Phosphoserine; by TRPM71 Publication
Cross-linki19 – 19Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
Modified residuei21 – 211Phosphotyrosine; by EGFR1 Publication
Modified residuei27 – 271Phosphoserine; by PKC1 Publication
Modified residuei34 – 341Phosphoserine1 Publication
Modified residuei37 – 371Phosphoserine1 Publication
Modified residuei58 – 581N6-acetyllysineBy similarity
Modified residuei239 – 2391N6-acetyllysine1 Publication
Modified residuei312 – 3121N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylated by protein kinase C, epidermal growth factor receptor/kinase and TRPM7. Phosphorylation results in loss of the inhibitory activity.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein

Proteomic databases

MaxQBiP04083.
PaxDbiP04083.
PeptideAtlasiP04083.
PRIDEiP04083.

2D gel databases

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

PTM databases

PhosphoSiteiP04083.

Expressioni

Gene expression databases

BgeeiP04083.
CleanExiHS_ANXA1.
ExpressionAtlasiP04083. baseline and differential.
GenevestigatoriP04083.

Organism-specific databases

HPAiCAB013023.
CAB035987.
CAB058693.
HPA011271.
HPA011272.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
IKBKGQ9Y6K96EBI-354007,EBI-81279
RIPK1Q135465EBI-354007,EBI-358507

Protein-protein interaction databases

BioGridi106798. 69 interactions.
DIPiDIP-32875N.
IntActiP04083. 60 interactions.
MINTiMINT-1212274.
STRINGi9606.ENSP00000257497.

Structurei

Secondary structure

1
346
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 108Combined sources
Helixi46 – 5510Combined sources
Beta strandi62 – 643Combined sources
Helixi65 – 717Combined sources
Helixi77 – 8711Combined sources
Helixi94 – 996Combined sources
Helixi106 – 1094Combined sources
Helixi110 – 1123Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AINX-ray2.50A33-346[»]
1BO9NMR-A41-113[»]
1QLSX-ray2.30D2-12[»]
ProteinModelPortaliP04083.
SMRiP04083. Positions 2-344.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04083.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati51 – 11161Annexin 1Add
BLAST
Repeati123 – 18361Annexin 2Add
BLAST
Repeati207 – 26761Annexin 3Add
BLAST
Repeati282 – 34261Annexin 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

eggNOGiNOG282829.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP04083.
KOiK17091.
OMAiMNDIKAC.
OrthoDBiEOG74XS72.
PhylomeDBiP04083.
TreeFamiTF105452.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002388. AnnexinI.
[Graphical view]
PANTHERiPTHR10502:SF17. PTHR10502:SF17. 1 hit.
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR00197. ANNEXINI.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04083-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMVSEFLKQ AWFIENEEQE YVQTVKSSKG GPGSAVSPYP TFNPSSDVAA
60 70 80 90 100
LHKAIMVKGV DEATIIDILT KRNNAQRQQI KAAYLQETGK PLDETLKKAL
110 120 130 140 150
TGHLEEVVLA LLKTPAQFDA DELRAAMKGL GTDEDTLIEI LASRTNKEIR
160 170 180 190 200
DINRVYREEL KRDLAKDITS DTSGDFRNAL LSLAKGDRSE DFGVNEDLAD
210 220 230 240 250
SDARALYEAG ERRKGTDVNV FNTILTTRSY PQLRRVFQKY TKYSKHDMNK
260 270 280 290 300
VLDLELKGDI EKCLTAIVKC ATSKPAFFAE KLHQAMKGVG TRHKALIRIM
310 320 330 340
VSRSEIDMND IKAFYQKMYG ISLCQAILDE TKGDYEKILV ALCGGN
Length:346
Mass (Da):38,714
Last modified:January 23, 2007 - v2
Checksum:i14B42E1FA4178EC0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05908 mRNA. Translation: CAA29338.1.
BC001275 mRNA. Translation: AAH01275.1.
BC035993 mRNA. Translation: AAH35993.1.
CCDSiCCDS6645.1.
PIRiA03080. LUHU.
RefSeqiNP_000691.1. NM_000700.2.
UniGeneiHs.494173.

Genome annotation databases

EnsembliENST00000257497; ENSP00000257497; ENSG00000135046.
ENST00000376911; ENSP00000366109; ENSG00000135046.
GeneIDi301.
KEGGihsa:301.
UCSCiuc004ajf.1. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05908 mRNA. Translation: CAA29338.1.
BC001275 mRNA. Translation: AAH01275.1.
BC035993 mRNA. Translation: AAH35993.1.
CCDSiCCDS6645.1.
PIRiA03080. LUHU.
RefSeqiNP_000691.1. NM_000700.2.
UniGeneiHs.494173.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AINX-ray2.50A33-346[»]
1BO9NMR-A41-113[»]
1QLSX-ray2.30D2-12[»]
ProteinModelPortaliP04083.
SMRiP04083. Positions 2-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106798. 69 interactions.
DIPiDIP-32875N.
IntActiP04083. 60 interactions.
MINTiMINT-1212274.
STRINGi9606.ENSP00000257497.

Chemistry

DrugBankiDB00288. Amcinonide.
DB01234. Dexamethasone.
DB00741. Hydrocortisone.

Protein family/group databases

TCDBi1.A.31.1.3. the annexin (annexin) family.

PTM databases

PhosphoSiteiP04083.

Polymorphism and mutation databases

BioMutaiANXA1.
DMDMi113944.

2D gel databases

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

Proteomic databases

MaxQBiP04083.
PaxDbiP04083.
PeptideAtlasiP04083.
PRIDEiP04083.

Protocols and materials databases

DNASUi301.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000257497; ENSP00000257497; ENSG00000135046.
ENST00000376911; ENSP00000366109; ENSG00000135046.
GeneIDi301.
KEGGihsa:301.
UCSCiuc004ajf.1. human.

Organism-specific databases

CTDi301.
GeneCardsiGC09P075766.
HGNCiHGNC:533. ANXA1.
HPAiCAB013023.
CAB035987.
CAB058693.
HPA011271.
HPA011272.
MIMi151690. gene.
neXtProtiNX_P04083.
PharmGKBiPA24823.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG282829.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP04083.
KOiK17091.
OMAiMNDIKAC.
OrthoDBiEOG74XS72.
PhylomeDBiP04083.
TreeFamiTF105452.

Enzyme and pathway databases

ReactomeiREACT_17044. Muscle contraction.
REACT_18283. G alpha (q) signalling events.
REACT_19231. G alpha (i) signalling events.
REACT_21264. Formyl peptide receptors bind formyl peptides and many other ligands.
SignaLinkiP04083.

Miscellaneous databases

ChiTaRSiANXA1. human.
EvolutionaryTraceiP04083.
GeneWikiiAnnexin_A1.
GenomeRNAii301.
NextBioi1213.
PROiP04083.
SOURCEiSearch...

Gene expression databases

BgeeiP04083.
CleanExiHS_ANXA1.
ExpressionAtlasiP04083. baseline and differential.
GenevestigatoriP04083.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002388. AnnexinI.
[Graphical view]
PANTHERiPTHR10502:SF17. PTHR10502:SF17. 1 hit.
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR00197. ANNEXINI.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "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).
  15. "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.

Entry informationi

Entry nameiANXA1_HUMAN
AccessioniPrimary (citable) accession number: P04083
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 197 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.