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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

Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity (PubMed:8425544). Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response (By similarity). Promotes resolution of inflammation and wound healing (PubMed:25664854). Functions at least in part by activating the formyl peptide receptors and downstream signaling cascades (PubMed:15187149, PubMed:25664854). Promotes chemotaxis of granulocytes and monocytes via activation of the formyl peptide receptors (PubMed:15187149). Contributes to the adaptive immune response by enhancing signaling cascades that are triggered by T-cell activation, regulates differentiation and proliferation of activated T-cells (PubMed:17008549). Promotes the differentiation of T-cells into Th1 cells and negatively regulates differentiation into Th2 cells (PubMed:17008549). Has no effect on unstimulated T cells (PubMed:17008549). Promotes rearrangement of the actin cytoskeleton, cell polarization and cell migration (PubMed:15187149). Negatively regulates hormone exocytosis via activation of the formyl peptide receptors and reorganization of the actin cytoskeleton (PubMed:19625660). Has high affinity for Ca2+ and can bind up to eight Ca2+ ions (By similarity). Displays Ca2+-dependent binding to phospholipid membranes (PubMed:2532504, PubMed:8557678). Plays a role in the formation of phagocytic cups and phagosomes. Plays a role in phagocytosis by mediating the Ca2+-dependent interaction between phagosomes and the actin cytoskeleton (By similarity).By similarity8 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi59 – 591Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi60 – 601Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi62 – 621Calcium 1By similarity
Metal bindingi97 – 971Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi100 – 1001Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi105 – 1051Calcium 2By similarity
Metal bindingi127 – 1271Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi129 – 1291Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi131 – 1311Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi132 – 1321Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi134 – 1341Calcium 4By similarity
Metal bindingi171 – 1711Calcium 3By similarity
Metal bindingi210 – 2101Calcium 5; via carbonyl oxygenBy similarity
Metal bindingi213 – 2131Calcium 5; via carbonyl oxygenBy similarity
Metal bindingi215 – 2151Calcium 5; via carbonyl oxygenBy similarity
Metal bindingi253 – 2531Calcium 6By similarity
Metal bindingi255 – 2551Calcium 5By similarity
Metal bindingi256 – 2561Calcium 6; via carbonyl oxygenBy similarity
Metal bindingi261 – 2611Calcium 6By similarity
Metal bindingi286 – 2861Calcium 7; via carbonyl oxygenBy similarity
Metal bindingi288 – 2881Calcium 7; via carbonyl oxygenBy similarity
Metal bindingi290 – 2901Calcium 7; via carbonyl oxygenBy similarity
Metal bindingi328 – 3281Calcium 8; via carbonyl oxygenBy similarity
Metal bindingi330 – 3301Calcium 7By similarity
Metal bindingi331 – 3311Calcium 8; via carbonyl oxygenBy similarity
Metal bindingi336 – 3361Calcium 8By similarity

GO - Molecular functioni

  • annealing helicase activity Source: Ensembl
  • calcium-dependent phospholipid binding Source: UniProtKB
  • calcium-dependent protein binding Source: AgBase
  • calcium ion binding Source: UniProtKB
  • 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

  • actin cytoskeleton reorganization Source: UniProtKB
  • adaptive immune response Source: UniProtKB-KW
  • 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
  • estrous cycle Source: Ensembl
  • gliogenesis Source: Ensembl
  • G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Source: UniProtKB
  • granulocyte chemotaxis Source: UniProtKB
  • hepatocyte differentiation Source: Ensembl
  • inflammatory response Source: UniProtKB
  • innate immune response Source: UniProtKB-KW
  • insulin secretion Source: Ensembl
  • keratinocyte differentiation Source: UniProtKB
  • monocyte chemotaxis Source: UniProtKB
  • myoblast migration involved in skeletal muscle regeneration Source: Ensembl
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of exocytosis Source: UniProtKB
  • negative regulation of interleukin-8 secretion Source: BHF-UCL
  • negative regulation of phospholipase A2 activity Source: Ensembl
  • negative regulation of T-helper 2 cell differentiation Source: UniProtKB
  • neutrophil clearance Source: BHF-UCL
  • neutrophil homeostasis Source: BHF-UCL
  • peptide cross-linking Source: UniProtKB
  • phagocytosis Source: UniProtKB
  • positive regulation of G1/S transition of mitotic cell cycle Source: Ensembl
  • positive regulation of interleukin-2 production Source: UniProtKB
  • positive regulation of neutrophil apoptotic process Source: Ensembl
  • positive regulation of prostaglandin biosynthetic process Source: Ensembl
  • positive regulation of T cell proliferation Source: UniProtKB
  • positive regulation of T-helper 1 cell differentiation Source: UniProtKB
  • positive regulation of vesicle fusion Source: UniProtKB
  • positive regulation of wound healing Source: UniProtKB
  • prolactin secretion Source: Ensembl
  • prostate gland development Source: Ensembl
  • regulation of cell shape Source: UniProtKB
  • regulation of hormone secretion Source: UniProtKB
  • regulation of inflammatory response Source: UniProtKB
  • regulation of interleukin-1 production Source: UniProtKB
  • regulation of leukocyte migration Source: UniProtKB
  • 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 - Biological processi

Adaptive immunity, Immunity, Inflammatory response, Innate immunity

Keywords - Ligandi

Calcium, Calcium/phospholipid-binding, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-397014. Muscle contraction.
R-HSA-416476. G alpha (q) signalling events.
R-HSA-418594. G alpha (i) signalling events.
R-HSA-444473. 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 I1 Publication
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

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB
  • basolateral plasma membrane Source: UniProtKB-SubCell
  • cell surface Source: BHF-UCL
  • cornified envelope Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • early endosome membrane Source: UniProtKB
  • endosome Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • extrinsic component of endosome membrane Source: UniProtKB
  • extrinsic component of external side of plasma membrane Source: UniProtKB
  • extrinsic component of membrane Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • lateral plasma membrane Source: UniProtKB
  • mast cell granule Source: Ensembl
  • mitochondrial membrane Source: Ensembl
  • motile cilium Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: BHF-UCL
  • phagocytic cup Source: UniProtKB-SubCell
  • 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, Cytoplasmic vesicle, Endosome, Membrane, Nucleus, Secreted

Pathology & Biotechi

Pharmaceutical usei

Peptides based on the N-terminal sequence might be used for the treatment of inflammation, e.g. in chronic bowel diseases and in rheumatoid arthritis.Curated

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi27 – 271S → A: Abolishes secretion and modulation of exocytosis. 1 Publication
Mutagenesisi34 – 341S → A: No effect on secretion and modulation of exocytosis. 1 Publication
Mutagenesisi45 – 451S → A: Abolishes secretion and nearly abolishes modulation of exocytosis. 1 Publication

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 methionineiRemoved1 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 – 341PhosphoserineCombined sources
Modified residuei37 – 371PhosphoserineCombined sources
Modified residuei58 – 581N6-acetyllysineBy similarity
Modified residuei239 – 2391N6-acetyllysineCombined sources
Cross-linki257 – 257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei312 – 3121N6-acetyllysineCombined sources
Disulfide bondi324 ↔ 343By similarity

Post-translational modificationi

Phosphorylated by protein kinase C, EGFR and TRPM7 (PubMed:2457390, PubMed:15485879). Phosphorylated in response to EGF treatment (PubMed:2532504).3 Publications
Sumoylated.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP04083.
PaxDbiP04083.
PeptideAtlasiP04083.
PRIDEiP04083.

2D gel databases

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

PTM databases

iPTMnetiP04083.
PhosphoSiteiP04083.

Expressioni

Tissue specificityi

Detected in resting neutrophils (PubMed:10772777). Detected in peripheral blood T-cells (PubMed:17008549). Detected in extracellular vesicles in blood serum from patients with inflammatory bowel disease, but not in serum from healthy donors (PubMed:25664854). Detected in placenta (at protein level) (PubMed:2532504). Detected in liver.2 Publications

Gene expression databases

BgeeiP04083.
CleanExiHS_ANXA1.
ExpressionAtlasiP04083. baseline and differential.
GenevisibleiP04083. HS.

Organism-specific databases

HPAiCAB013023.
CAB035987.
CAB058693.
HPA011271.
HPA011272.

Interactioni

Subunit structurei

Homodimer; non-covalently linked (By similarity). Homodimer; linked by transglutamylation (PubMed:2532504). Homodimers linked by transglutamylation are observed in placenta, but not in other tissues (PubMed:2532504). Interacts with S100A11 (PubMed:8557678, PubMed:10673436). Heterotetramer, formed by two molecules each of S100A11 and ANXA1 (PubMed:10673436). Interacts with DYSF (By similarity). Interacts with EGFR (By similarity).By similarity3 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi106798. 72 interactions.
DIPiDIP-32875N.
IntActiP04083. 72 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

The full-length protein can bind eight Ca2+ 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 Ca2+, these sites are buried in the interior of the protein core. The N-terminal region becomes disordered in response to calcium-binding.By similarity
The N-terminal 26 amino acids are sufficient for its extracellular functions in the regulation of inflammation and wound healing (PubMed:25664854). Acylated peptides that contain the first 26 amino acids of the mature protein can activate signaling via the formyl peptide receptors (PubMed:15187149, PubMed:25664854).2 Publications

Sequence similaritiesi

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

Keywords - Domaini

Annexin, Repeat

Phylogenomic databases

eggNOGiKOG0819. Eukaryota.
ENOG410XPUN. LUCA.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP04083.
KOiK17091.
OMAiIMVSRHE.
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.
XP_011516911.1. XM_011518609.1.
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.
XP_011516911.1. XM_011518609.1.
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. 72 interactions.
DIPiDIP-32875N.
IntActiP04083. 72 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

iPTMnetiP04083.
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.
GeneCardsiANXA1.
HGNCiHGNC:533. ANXA1.
HPAiCAB013023.
CAB035987.
CAB058693.
HPA011271.
HPA011272.
MIMi151690. gene.
neXtProtiNX_P04083.
PharmGKBiPA24823.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0819. Eukaryota.
ENOG410XPUN. LUCA.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP04083.
KOiK17091.
OMAiIMVSRHE.
OrthoDBiEOG74XS72.
PhylomeDBiP04083.
TreeFamiTF105452.

Enzyme and pathway databases

ReactomeiR-HSA-397014. Muscle contraction.
R-HSA-416476. G alpha (q) signalling events.
R-HSA-418594. G alpha (i) signalling events.
R-HSA-444473. 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.
GenevisibleiP04083. HS.

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], FUNCTION, TISSUE SPECIFICITY.
  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], FUNCTION.
  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: FUNCTION, DIMERIZATION, SUBUNIT, TISSUE SPECIFICITY, PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION, SUBCELLULAR LOCATION.
  8. "Calcium-dependent binding of S100C to the N-terminal domain of annexin I."
    Mailliard W.S., Haigler H.T., Schlaepfer D.D.
    J. Biol. Chem. 271:719-725(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH S100A11, FUNCTION, SUBCELLULAR LOCATION.
  9. "Annexin I is stored within gelatinase granules of human neutrophil and mobilized on the cell surface upon adhesion but not phagocytosis."
    Perretti M., Christian H., Wheller S.K., Aiello I., Mugridge K.G., Morris J.F., Flower R.J., Goulding N.J.
    Cell Biol. Int. 24:163-174(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  10. "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.
  11. "An annexin 1 N-terminal peptide activates leukocytes by triggering different members of the formyl peptide receptor family."
    Ernst S., Lange C., Wilbers A., Goebeler V., Gerke V., Rescher U.
    J. Immunol. 172:7669-7676(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN.
  12. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  13. "Annexin-A1: a pivotal regulator of the innate and adaptive immune systems."
    D'Acquisto F., Perretti M., Flower R.J.
    Br. J. Pharmacol. 155:152-169(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Annexin A1 regulates hormone exocytosis through a mechanism involving actin reorganization."
    McArthur S., Yazid S., Christian H., Sirha R., Flower R., Buckingham J., Solito E.
    FASEB J. 23:4000-4010(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-27; SER-34 AND SER-45.
  16. "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].
  17. "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.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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.
  20. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN.
  21. "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) IN COMPLEX WITH CALCIUM IONS, CALCIUM-BINDING.
  22. "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.
  23. "Structural basis of the Ca(2+)-dependent association between S100C (S100A11) and its target, the N-terminal part of annexin I."
    Rety S., Osterloh D., Arie J.-P., Tabaries S., Seeman J., Russo-Marie F., Gerke V., Lewit-Bentley A.
    Structure 8:175-184(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-12 IN COMPLEX WITH S100A11, INTERACTION WITH S100A11.

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: January 20, 2016
This is version 204 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

Miscellaneous

Was originally identified as calcium and phospholipid binding protein that displays Ca2+-dependent binding to phospholipid membranes and can promote membrane aggregation in vitro. Was initially identified as inhibitor of phospholipase A2 activity (in vitro) (PubMed:2936963, PubMed:8425544). Inhibition of phospholipase activity is mediated via its phospholipid binding activity that limits the access of phospholipase to its substrates.Curated2 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Pharmaceutical, 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

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 one 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.