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Protein

Annexin A1

Gene

Anxa1

Organism
Mus musculus (Mouse)
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:12475898). Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response (PubMed:12475898). Promotes resolution of inflammation and wound healing (PubMed:25664854). Functions at least in part by activating the formyl peptide receptors and downstream signaling cascades. Promotes chemotaxis of granulocytes and monocytes via activation of the formyl peptide receptors (By similarity). 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:17948261). Promotes the differentiation of T-cells into Th1 cells and negatively regulates differentiation into Th2 cells (PubMed:17948261). Has no effect on unstimulated T-cells. Promotes rearrangement of the actin cytoskeleton, cell polarization and cell migration. Negatively regulates hormone exocytosis via activation of the formyl peptide receptors and reorganization of the actin cytoskeleton (By similarity). Has high affinity for Ca2+ and can bind up to eight Ca2+ ions (By similarity). Displays Ca2+-dependent binding to phospholipid membranes (By similarity). Plays a role in the formation of phagocytic cups and phagosomes (PubMed:21245195). Plays a role in phagocytosis by mediating the Ca2+-dependent interaction between phagosomes and the actin cytoskeleton (PubMed:21245195).By similarity4 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

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: MGI
  • cell surface receptor signaling pathway Source: Ensembl
  • cellular response to glucocorticoid stimulus Source: UniProtKB
  • 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: MGI
  • monocyte chemotaxis Source: UniProtKB
  • myoblast migration involved in skeletal muscle regeneration Source: CACAO
  • negative regulation of exocytosis Source: UniProtKB
  • negative regulation of interleukin-8 secretion Source: MGI
  • negative regulation of phospholipase A2 activity Source: Ensembl
  • negative regulation of T-helper 2 cell differentiation Source: UniProtKB
  • neutrophil clearance Source: MGI
  • neutrophil homeostasis Source: BHF-UCL
  • peptide cross-linking Source: MGI
  • phagocytosis Source: UniProtKB
  • positive regulation of G1/S transition of mitotic cell cycle Source: MGI
  • positive regulation of interleukin-2 production Source: UniProtKB
  • positive regulation of neutrophil apoptotic process Source: BHF-UCL
  • 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: MGI
  • positive regulation of wound healing Source: UniProtKB
  • prolactin secretion Source: Ensembl
  • prostate gland development Source: Ensembl
  • regulation of cell proliferation Source: MGI
  • 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: MGI
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-MMU-416476. G alpha (q) signalling events.
R-MMU-418594. G alpha (i) signalling events.
R-MMU-444473. Formyl peptide receptors bind formyl peptides and many other ligands.

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, Lpc-1, Lpc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:96819. Anxa1.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB
  • basolateral plasma membrane Source: UniProtKB-SubCell
  • cell surface Source: MGI
  • cornified envelope Source: MGI
  • cytoplasm Source: UniProtKB
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • cytosol Source: Reactome
  • early endosome membrane Source: UniProtKB
  • endosome Source: MGI
  • extracellular exosome Source: UniProtKB
  • 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: MGI
  • focal adhesion Source: MGI
  • lateral plasma membrane Source: UniProtKB
  • mast cell granule Source: Ensembl
  • mitochondrial membrane Source: Ensembl
  • motile cilium Source: UniProtKB
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • phagocytic cup Source: UniProtKB-SubCell
  • plasma membrane Source: CACAO
  • protein complex Source: Ensembl
  • sarcolemma Source: MGI
  • vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Cytoplasm, Cytoplasmic vesicle, Endosome, Membrane, Nucleus, Secreted

Pathology & Biotechi

Disruption phenotypei

Mice are born at the expected Mendelian rate, appear healthy and are fertile, but tend to die already after about one year. Mutant mice display an increased inflammatory response during zymosan-induced peritonitis, with increased blood leukocyte migration and increased production of IL1B. In mutant mice, glucocorticoid-mediated down-regulation of the early phase of the inflammatory response is abolished, but there is no effect on glucocorticoid-mediated down-regulation of later phases of the inflammatory response. Peritoneal lavage macrophages from mutant mice display decreased phagocytosis. Besides, glucocorticoid-mediated inhibition of phagocytosis is abolished (PubMed:12475898). Mutant mice display increased susceptibility to dextran sulfate sodium (DSS)-induced colitis with increased mucosal injury, slower recovery and increased morbidity (PubMed:18802107). Mutant mice have an exacerbated allergic response after exposure to ovalbumin (PubMed:17948261). T-cells from mutant mice show skewed differentiation into Th1 and Th2 cells with increased differentiation into Th2 cells and decreased differentiation into Th1 cells (PubMed:17948261).3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi257 – 2571K → R: Strongly decreased sumoylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 346345Annexin A1PRO_0000067461Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei5 – 51Phosphoserine; by TRPM7By similarity
Cross-linki19 – 19Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Modified residuei21 – 211PhosphotyrosineCombined sources
Modified residuei27 – 271Phosphoserine; by PKCBy similarity
Modified residuei34 – 341PhosphoserineBy similarity
Modified residuei37 – 371PhosphoserineBy similarity
Modified residuei58 – 581N6-acetyllysineCombined sources
Cross-linki214 – 214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki257 – 257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
Modified residuei312 – 3121N6-acetyllysineCombined sources
Disulfide bondi324 ↔ 343By similarity

Post-translational modificationi

Phosphorylated by protein kinase C, EGFR and TRPM7. Phosphorylated in response to EGF treatment.By similarity
Sumoylated.1 Publication

Keywords - PTMi

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

Proteomic databases

EPDiP10107.
PaxDbiP10107.
PRIDEiP10107.

2D gel databases

COMPLUYEAST-2DPAGEP10107.

PTM databases

iPTMnetiP10107.
PhosphoSiteiP10107.

Expressioni

Tissue specificityi

Detected in lung (PubMed:12475898, PubMed:17384087). Detected at the apical membrane of airway epithelial cells (PubMed:17384087). Detected in intestinal epithelial cells (PubMed:18802107). Detected in skeletal muscle (PubMed:14506282). Detected in prostate (PubMed:23727357). Detected in thymus (at protein level) (PubMed:12475898). Detected in stomach, lung, spleen, ovary and uterus, and at lower levels in kidney, thymus and heart (PubMed:12475898).4 Publications

Inductioni

Up-regulated by the synthetic glucocorticoid fluocinolone acetonide.1 Publication

Gene expression databases

BgeeiP10107.
CleanExiMM_ANXA1.
ExpressionAtlasiP10107. baseline and differential.
GenevisibleiP10107. MM.

Interactioni

Subunit structurei

Homodimer; non-covalently linked (By similarity). Homodimer; linked by transglutamylation. Homodimers linked by transglutamylation are observed in placenta, but not in other tissues. Interacts with S100A11. Heterotetramer, formed by two molecules each of S100A11 and ANXA1 (By similarity). Interacts with DYSF (PubMed:14506282). Interacts with EGFR (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi201194. 4 interactions.
IntActiP10107. 7 interactions.
MINTiMINT-274958.
STRINGi10090.ENSMUSP00000025561.

Structurei

3D structure databases

ProteinModelPortaliP10107.
SMRiP10107. Positions 2-344.
ModBaseiSearch...
MobiDBiSearch...

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. Acylated peptides that contain the first 26 amino acids of the mature protein can activate signaling via the formyl peptide receptors.By similarity

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.
InParanoidiP10107.
KOiK17091.
OMAiIMVSRHE.
OrthoDBiEOG74XS72.
PhylomeDBiP10107.
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.

P10107-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMVSEFLKQ ARFLENQEQE YVQAVKSYKG GPGSAVSPYP SFNVSSDVAA
60 70 80 90 100
LHKAIMVKGV DEATIIDILT KRTNAQRQQI KAAYLQENGK PLDEVLRKAL
110 120 130 140 150
TGHLEEVVLA MLKTPAQFDA DELRGAMKGL GTDEDTLIEI LTTRSNEQIR
160 170 180 190 200
EINRVYREEL KRDLAKDITS DTSGDFRKAL LALAKGDRCQ DLSVNQDLAD
210 220 230 240 250
TDARALYEAG ERRKGTDVNV FTTILTSRSF PHLRRVFQNY GKYSQHDMNK
260 270 280 290 300
ALDLELKGDI EKCLTTIVKC ATSTPAFFAE KLYEAMKGAG TRHKALIRIM
310 320 330 340
VSRSEIDMNE IKVFYQKKYG ISLCQAILDE TKGDYEKILV ALCGGN
Length:346
Mass (Da):38,734
Last modified:January 23, 2007 - v2
Checksum:i9393A11B24191D3C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 792QQ → PR in AAA39420 (PubMed:2522299).Curated
Sequence conflicti212 – 2121R → I in AAA39437 (PubMed:1676980).Curated
Sequence conflicti222 – 2221T → H in AAA39420 (PubMed:2522299).Curated
Sequence conflicti274 – 2741T → H in AAA39420 (PubMed:2522299).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07486 mRNA. Translation: CAA30371.1.
M69260
, M69250, M69251, M69252, M69253, M69254, M69255, M69256, M69257, M69258, M69259 Genomic DNA. Translation: AAA39437.1.
BC002289 mRNA. Translation: AAH02289.1.
BC004594 mRNA. Translation: AAH04594.1.
M24554 mRNA. Translation: AAA39420.1.
CCDSiCCDS29692.1.
PIRiS02181. LUMS1.
RefSeqiNP_034860.2. NM_010730.2.
UniGeneiMm.248360.

Genome annotation databases

EnsembliENSMUST00000025561; ENSMUSP00000025561; ENSMUSG00000024659.
GeneIDi16952.
KEGGimmu:16952.
UCSCiuc008gyi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07486 mRNA. Translation: CAA30371.1.
M69260
, M69250, M69251, M69252, M69253, M69254, M69255, M69256, M69257, M69258, M69259 Genomic DNA. Translation: AAA39437.1.
BC002289 mRNA. Translation: AAH02289.1.
BC004594 mRNA. Translation: AAH04594.1.
M24554 mRNA. Translation: AAA39420.1.
CCDSiCCDS29692.1.
PIRiS02181. LUMS1.
RefSeqiNP_034860.2. NM_010730.2.
UniGeneiMm.248360.

3D structure databases

ProteinModelPortaliP10107.
SMRiP10107. Positions 2-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201194. 4 interactions.
IntActiP10107. 7 interactions.
MINTiMINT-274958.
STRINGi10090.ENSMUSP00000025561.

PTM databases

iPTMnetiP10107.
PhosphoSiteiP10107.

2D gel databases

COMPLUYEAST-2DPAGEP10107.

Proteomic databases

EPDiP10107.
PaxDbiP10107.
PRIDEiP10107.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025561; ENSMUSP00000025561; ENSMUSG00000024659.
GeneIDi16952.
KEGGimmu:16952.
UCSCiuc008gyi.1. mouse.

Organism-specific databases

CTDi301.
MGIiMGI:96819. Anxa1.

Phylogenomic databases

eggNOGiKOG0819. Eukaryota.
ENOG410XPUN. LUCA.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP10107.
KOiK17091.
OMAiIMVSRHE.
OrthoDBiEOG74XS72.
PhylomeDBiP10107.
TreeFamiTF105452.

Enzyme and pathway databases

ReactomeiR-MMU-416476. G alpha (q) signalling events.
R-MMU-418594. G alpha (i) signalling events.
R-MMU-444473. Formyl peptide receptors bind formyl peptides and many other ligands.

Miscellaneous databases

ChiTaRSiAnxa1. mouse.
NextBioi291004.
PROiP10107.
SOURCEiSearch...

Gene expression databases

BgeeiP10107.
CleanExiMM_ANXA1.
ExpressionAtlasiP10107. baseline and differential.
GenevisibleiP10107. MM.

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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Mouse lipocortin I gene structure and chromosomal assignment: gene duplication and the origins of a gene family."
    Horlick K.R., Cheng I.C., Wong W.T., Wakeland E.K., Nick H.S.
    Genomics 10:365-374(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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].
    Strain: Czech II.
    Tissue: Mammary gland.
  4. "cDNA-cloning, sequencing and expression in glucocorticoid-stimulated quiescent Swiss 3T3 fibroblasts of mouse lipocortin I."
    Philipps C., Rose-John S., Rincke G., Fuerstenberger G., Marks F.
    Biochem. Biophys. Res. Commun. 159:155-162(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-346, INDUCTION BY GLUCOCORTICOIDS.
  5. Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
  6. "Dysferlin interacts with annexins A1 and A2 and mediates sarcolemmal wound-healing."
    Lennon N.J., Kho A., Bacskai B.J., Perlmutter S.L., Hyman B.T., Brown R.H. Jr.
    J. Biol. Chem. 278:50466-50473(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DYSF, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "CCSP regulates cross talk between secretory cells and both ciliated cells and macrophages of the conducting airway."
    Reynolds S.D., Reynolds P.R., Snyder J.C., Whyte F., Paavola K.J., Stripp B.R.
    Am. J. Physiol. 293:L114-L123(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
  8. "Impaired T cell activation and increased Th2 lineage commitment in Annexin-1-deficient T cells."
    D'Acquisto F., Paschalidis N., Sampaio A.L., Merghani A., Flower R.J., Perretti M.
    Eur. J. Immunol. 37:3131-3142(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  9. "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.
  10. Cited for: DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  12. "Annexin A1 and glucocorticoids as effectors of the resolution of inflammation."
    Perretti M., D'Acquisto F.
    Nat. Rev. Immunol. 9:62-70(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  14. "Annexin A1 is a new functional linker between actin filaments and phagosomes during phagocytosis."
    Patel D.M., Ahmad S.F., Weiss D.G., Gerke V., Kuznetsov S.A.
    J. Cell Sci. 124:578-588(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  15. "Annexin A1 is regulated by domains cross-talk through post-translational phosphorylation and SUMOYlation."
    Caron D., Maaroufi H., Michaud S., Tanguay R.M., Faure R.L.
    Cell. Signal. 25:1962-1969(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-257, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF LYS-257.
  16. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58 AND LYS-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  17. Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiANXA1_MOUSE
AccessioniPrimary (citable) accession number: P10107
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 166 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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). Inhibition of phospholipase activity is mediated via its phospholipid binding activity that limits the access of phospholipase to its substrates.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.