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P04083

- ANXA1_HUMAN

UniProt

P04083 - ANXA1_HUMAN

Protein

Annexin A1

Gene

ANXA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 189 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

    1. calcium-dependent phospholipid binding Source: UniProtKB
    2. calcium-dependent protein binding Source: AgBase
    3. calcium ion binding Source: ProtInc
    4. phospholipase A2 inhibitor activity Source: UniProtKB
    5. phospholipid binding Source: ProtInc
    6. protein binding Source: IntAct
    7. protein binding, bridging Source: UniProtKB
    8. receptor binding Source: ProtInc
    9. structural molecule activity Source: UniProtKB

    GO - Biological processi

    1. alpha-beta T cell differentiation Source: BHF-UCL
    2. arachidonic acid secretion Source: Ensembl
    3. cell surface receptor signaling pathway Source: ProtInc
    4. cellular component movement Source: ProtInc
    5. cellular response to glucocorticoid stimulus Source: BHF-UCL
    6. cellular response to hydrogen peroxide Source: Ensembl
    7. endocrine pancreas development Source: Ensembl
    8. estrous cycle phase Source: Ensembl
    9. gliogenesis Source: Ensembl
    10. hepatocyte differentiation Source: Ensembl
    11. inflammatory response Source: ProtInc
    12. insulin secretion Source: Ensembl
    13. keratinocyte differentiation Source: UniProtKB
    14. negative regulation of acute inflammatory response Source: Ensembl
    15. negative regulation of apoptotic process Source: UniProtKB
    16. negative regulation of catalytic activity Source: GOC
    17. negative regulation of interleukin-8 secretion Source: BHF-UCL
    18. neutrophil clearance Source: BHF-UCL
    19. neutrophil homeostasis Source: BHF-UCL
    20. peptide cross-linking Source: UniProtKB
    21. positive regulation of G1/S transition of mitotic cell cycle Source: Ensembl
    22. positive regulation of neutrophil apoptotic process Source: Ensembl
    23. positive regulation of prostaglandin biosynthetic process Source: Ensembl
    24. positive regulation of vesicle fusion Source: UniProtKB
    25. regulation of cell proliferation Source: Ensembl
    26. response to drug Source: Ensembl
    27. response to estradiol Source: Ensembl
    28. response to interleukin-1 Source: Ensembl
    29. response to peptide hormone Source: Ensembl
    30. response to X-ray Source: Ensembl
    31. signal transduction Source: UniProtKB

    Keywords - Molecular functioni

    Phospholipase A2 inhibitor

    Keywords - Ligandi

    Calcium, Calcium/phospholipid-binding

    Enzyme and pathway databases

    ReactomeiREACT_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: 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

    1. basolateral plasma membrane Source: UniProtKB-SubCell
    2. cell surface Source: BHF-UCL
    3. cilium Source: UniProtKB-SubCell
    4. cornified envelope Source: UniProtKB
    5. cytoplasm Source: UniProtKB
    6. extracellular region Source: Reactome
    7. extracellular space Source: UniProt
    8. extracellular vesicular exosome Source: UniProtKB
    9. mitochondrial membrane Source: Ensembl
    10. nucleus Source: BHF-UCL
    11. plasma membrane Source: HPA
    12. protein complex Source: Ensembl
    13. sarcolemma Source: Ensembl
    14. vesicle Source: UniProtKB

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24823.

    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 residuei24 – 241Phosphothreonine
    Modified residuei27 – 271Phosphoserine; by PKC1 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.3 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

    ArrayExpressiP04083.
    BgeeiP04083.
    CleanExiHS_ANXA1.
    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. 53 interactions.
    DIPiDIP-32875N.
    IntActiP04083. 59 interactions.
    MINTiMINT-1212274.
    STRINGi9606.ENSP00000257497.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiGTRHKTL.
    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]
    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

    MAMVSEFLKQ AWFIENEEQE YVQTVKSSKG GPGSAVSPYP TFNPSSDVAA    50
    LHKAIMVKGV DEATIIDILT KRNNAQRQQI KAAYLQETGK PLDETLKKAL 100
    TGHLEEVVLA LLKTPAQFDA DELRAAMKGL GTDEDTLIEI LASRTNKEIR 150
    DINRVYREEL KRDLAKDITS DTSGDFRNAL LSLAKGDRSE DFGVNEDLAD 200
    SDARALYEAG ERRKGTDVNV FNTILTTRSY PQLRRVFQKY TKYSKHDMNK 250
    VLDLELKGDI EKCLTAIVKC ATSKPAFFAE KLHQAMKGVG TRHKALIRIM 300
    VSRSEIDMND IKAFYQKMYG ISLCQAILDE TKGDYEKILV ALCGGN 346
    Length:346
    Mass (Da):38,714
    Last modified:January 23, 2007 - v2
    Checksum:i14B42E1FA4178EC0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_000700.1.
    UniGeneiHs.494173.

    Genome annotation databases

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

    Polymorphism databases

    DMDMi113944.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05908 mRNA. Translation: CAA29338.1 .
    BC001275 mRNA. Translation: AAH01275.1 .
    BC035993 mRNA. Translation: AAH35993.1 .
    CCDSi CCDS6645.1.
    PIRi A03080. LUHU.
    RefSeqi NP_000691.1. NM_000700.1.
    UniGenei Hs.494173.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AIN X-ray 2.50 A 33-346 [» ]
    1BO9 NMR - A 41-113 [» ]
    1QLS X-ray 2.30 D 2-12 [» ]
    ProteinModelPortali P04083.
    SMRi P04083. Positions 2-344.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106798. 53 interactions.
    DIPi DIP-32875N.
    IntActi P04083. 59 interactions.
    MINTi MINT-1212274.
    STRINGi 9606.ENSP00000257497.

    Chemistry

    DrugBanki DB00288. Amcinonide.
    DB01234. Dexamethasone.
    DB00741. Hydrocortisone.

    Protein family/group databases

    TCDBi 1.A.31.1.3. the annexin (annexin) family.

    PTM databases

    PhosphoSitei P04083.

    Polymorphism databases

    DMDMi 113944.

    2D gel databases

    DOSAC-COBS-2DPAGE P04083.
    REPRODUCTION-2DPAGE IPI00218918.
    P04083.
    UCD-2DPAGE P04083.

    Proteomic databases

    MaxQBi P04083.
    PaxDbi P04083.
    PeptideAtlasi P04083.
    PRIDEi P04083.

    Protocols and materials databases

    DNASUi 301.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000257497 ; ENSP00000257497 ; ENSG00000135046 .
    ENST00000376911 ; ENSP00000366109 ; ENSG00000135046 .
    GeneIDi 301.
    KEGGi hsa:301.
    UCSCi uc004ajf.1. human.

    Organism-specific databases

    CTDi 301.
    GeneCardsi GC09P075766.
    HGNCi HGNC:533. ANXA1.
    HPAi CAB013023.
    CAB035987.
    CAB058693.
    HPA011271.
    HPA011272.
    MIMi 151690. gene.
    neXtProti NX_P04083.
    PharmGKBi PA24823.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG282829.
    HOGENOMi HOG000158803.
    HOVERGENi HBG061815.
    InParanoidi P04083.
    KOi K17091.
    OMAi GTRHKTL.
    OrthoDBi EOG74XS72.
    PhylomeDBi P04083.
    TreeFami TF105452.

    Enzyme and pathway databases

    Reactomei 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.
    SignaLinki P04083.

    Miscellaneous databases

    ChiTaRSi ANXA1. human.
    EvolutionaryTracei P04083.
    GeneWikii Annexin_A1.
    GenomeRNAii 301.
    NextBioi 1213.
    PROi P04083.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P04083.
    Bgeei P04083.
    CleanExi HS_ANXA1.
    Genevestigatori P04083.

    Family and domain databases

    Gene3Di 1.10.220.10. 4 hits.
    InterProi IPR001464. Annexin.
    IPR018502. Annexin_repeat.
    IPR018252. Annexin_repeat_CS.
    IPR002388. AnnexinI.
    [Graphical view ]
    Pfami PF00191. Annexin. 4 hits.
    [Graphical view ]
    PRINTSi PR00196. ANNEXIN.
    PR00197. ANNEXINI.
    SMARTi SM00335. ANX. 4 hits.
    [Graphical view ]
    PROSITEi PS00223. ANNEXIN. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.

    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: October 1, 2014
    This is version 189 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