Protein detail

ANXA1

Annexin A1 (Annexin I) (Annexin-1) (Calpactin II) (Calpactin-2) (Chromobindin-9) (Lipocortin I) (Phospholipase A2 inhibitory protein) (p35) [Cleaved into: Annexin Ac2-26]

Protein symbol
ANXA1
UniProt ID
EVMP score
0.63
Frequency
10
Transmembrane count
Protein classification
Cancer-related genesFDA approved drug targetsPlasma proteinsPredicted intracellular proteinsPredicted secreted proteinsTransporters
Basic Information
Protein Names
Annexin A1 (Annexin I) (Annexin-1) (Calpactin II) (Calpactin-2) (Chromobindin-9) (Lipocortin I) (Phospholipase A2 inhibitory protein) (p35) [Cleaved into: Annexin Ac2-26]
Protein Class
Cancer-related genesFDA approved drug targetsPlasma proteinsPredicted intracellular proteinsPredicted secreted proteinsTransporters
Protein Function
  • Predicted intracellular proteins
  • Transporters:Transporter channels and pores
  • Cancer-related genes:Candidate cancer biomarkers
  • Predicted secreted proteins
  • FDA approved drug targets:Small molecule drugs
Entrez Gene Symbol
Gene Synonym
ANX1LPC1
Gene Description
Annexin A1
Chromosome
9
Position
73151865-73170393
Frequency
10
EVMP Score
0.63
Fluorescence & Localization
Tissue SpecificbrainCell SpecificAlveolar cells type 1Single-Nuclei Brain Specificdeep-layer near-projecting
Function & Pathway
Protein Function
  • Predicted intracellular proteins
  • Transporters:Transporter channels and pores
  • Cancer-related genes:Candidate cancer biomarkers
  • Predicted secreted proteins
  • FDA approved drug targets:Small molecule drugs
Mediation Categories
Adhesion and uptake mediationClinical-translation mediationFusion and delivery mediationImmune mediationReceptor-signaling mediation
Relations & Evidence

Enzyme-Mediated Modification

29 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
ANXA1PRKCHP24723S27phosphorylationSIGNOR_ProtMapperSIGNORProtMapperSIGNOR:24103589ProtMapper:24103589
ANXA1PRKCBP05771S27phosphorylationphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperKEASIGNOR_ProtMapperKEA:17570479SIGNOR:24103589ProtMapper:24103589
ANXA1PRKCBP05771S28phosphorylationphosphoELM_MIMPPhosphoSite_MIMPMIMPProtMapperPhosphoSitePhosphoSite_ProtMapper
ANXA1PRKCBP05771T24phosphorylationMIMPphosphoELM_MIMP
ANXA1TRPM7Q96QT4S5phosphorylationSparser_ProtMapperphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPProtMapperHPRDRLIMS-P_ProtMapperKEASIGNOR_ProtMapperREACH_ProtMapperPhosphoSitePhosphoSite_ProtMapperHPRD:15485879ProtMapper:26218331ProtMapper:24103589ProtMapper:21280599ProtMapper:15485879HPRD:20068231ProtMapper:24465463KEA:15485879ProtMapper:20180991ProtMapper:20932259
ANXA1PRKACAP17612T216phosphorylationphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPProtMapperPhosphoSitePhosphoSite_ProtMapper
ANXA1PRKCDQ05655S27phosphorylationMIMPHPRD_MIMPphosphoELM_MIMPPhosphoSite_MIMP
ANXA1PRKCDQ05655S28phosphorylationMIMPphosphoELM_MIMPPhosphoSite_MIMP
ANXA1PRKCDQ05655T24phosphorylationMIMPphosphoELM_MIMP
ANXA1PRKCEQ02156S27phosphorylationMIMPHPRD_MIMPphosphoELM_MIMPPhosphoSite_MIMP
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Ligand-Receptor Signaling

45 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
receptorreceptorGO_IntercellNoYesYesNoNo
receptorreceptorBaccin2019NoYesYesNoNo
receptorreceptorOmniPathNoYesYesNoNo
extracellularextracellularHPMRNoNoYesNoNo
extracellularextracellularOmniPathNoNoYesNoNo
intracellularintracellularComPPINoNoYesNoNo
intracellularintracellularGO_IntercellNoNoYesNoNo
intracellularintracellularUniProt_locationNoNoYesNoNo
intracellularintracellularOmniPathNoNoYesNoNo
cell_surface_ligandcell_surface_ligandconnectomeDB2020YesNoYesNoNo
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Regulatory Interaction Network

11 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
EGFRP00533ANXA1P04083YesYesNoHPRD_MIMPSIGNORProtMapperdbPTMHINTPhosphoSite_KEAphosphoELM_KEALit-BM-17HPRDIntActPhosphoSite_ProtMapperphosphoELM_MIMPPhosphoSite_MIMPMIMPiPTMnetPhosphoPointKEAphosphoELMSIGNOR_ProtMapperPhosphoSiteSparser_ProtMapperSPIKE_LCHINT:20029029Lit-BM-17:15581623PhosphoSite:2457390HINT:15581623Lit-BM-17:24189400PhosphoSite:24782913KEA:2457390ProtMapper:34208346SIGNOR:24103589IntAct:20029029ProtMapper:24103589dbPTM:17081983dbPTM:2457390phosphoELM:2457390ProtMapper:9223619PhosphoSite:16052208Lit-BM-17:20029029IntAct:31980649SPIKE_LC:15581623IntAct:15581623HPRD:15581623KEA:3020049
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Protein Complex Composition

11 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
SPANXA1Q9NS260hu.MAP2
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Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationUltrafiltration / Tangential Flow FiltrationSize Exclusion ChromatographyImmunoaffinity CaptureMass spectrometrySmall R sequencing (Illumi HiSeq 2000 (Solexa)1638590132379267563606464738113368373224753330447841068253335925003801459530915084329169863614683438207106390017003698231237670049
Sequence, Structure & Domains

Sequences

Length
346
Mass
38,714
Sequence
MAMVSEFLKQAWFIENEEQEYVQTVKSSKGGPGSAVSPYPTFNPSSDVAALHKAIMVKGVDEATIIDILTKRNNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLALLKTPAQFDADELRAAMKGLGTDEDTLIEILASRTNKEIRDINRVYREELKRDLAKDITSDTSGDFRNALLSLAKGDRSEDFGVNEDLADSDARALYEAGERRKGTDVNVFNTILTTRSYPQLRRVFQKYTKYSKHDMNKVLDLELKGDIEKCLTAIVKCATSKPAFFAEKLHQAMKGVGTRHKALIRIMVSRSEIDMNDIKAFYQKMYGISLCQAILDETKGDYEKILVALCGGN

3D Structural Models

Helix
3..10; 16..18; 46..55; 65..71; 77..87; 94..99; 106..109; 110..112
Beta Strand
62..64
3D Structure
NMR spectroscopy (2); X-ray crystallography (2)

Domain & Motif Annotations

Repeat
42..113; Annexin 1; 114..185; Annexin 2; 197..269; Annexin 3; 273..344; Annexin 4
Domain (CC)
The full-length protein can bind eight Ca(2+) ions via the annexin repeats. Calcium binding causes a major conformation change that modifies dimer contacts and leads to surface exposure of the N-terminal phosphorylation sites; in the absence of Ca(2+), these sites are buried in the interior of the protein core. The N-terminal region becomes disordered in response to calcium-binding.
Protein Families
Annexin family
Sequence Similarities
Belongs to the annexin family.
Clinical Relevance