Search Results

Overview

Uniprot IDP07150
Protein NameAnnexin A1
Gene NameAnxa1
OrganismRattus norvegicus

Kla Sites from experimental identification

Position Flanking peptide
128 DELRAAMKGLGTDED
16 KQACYIEKQEQEYVQ
166 ELKRDLAKDITSDTS
185 NALLALAKGDRCEDM
214 YEAGERRKGTDVNVF
235 RSYPHLRKVFQNYRK
242 KVFQNYRKYSQHDMN
250 YSQHDMNKALDLELK
257 KALDLELKGDIEKCL
26 QEYVQAVKSYKGGPG
262 ELKGDIEKCLTTIVK
287 EKLYEAMKGAGTRHK
29 VQAVKSYKGGPGSAV
312 EIDMNEIKVFYQKKY
318 IKVFYQKKYGIPLCQ
53 SDVAALHKAIMVKGV
58 LHKAIMVKGVDEATI
71 TIIDILTKRTNAQRQ
81 NAQRQQIKAAYLQET
90 AYLQETGKPLDETLK
97 KPLDETLKKALTGHL
98 PLDETLKKALTGHLE

Function

Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity. Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response. 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. Promotes the differentiation of T cells into Th1 cells and negatively regulates differentiation into Th2 cells (By similarity). Has no effect on unstimulated T cells. Negatively regulates hormone exocytosis via activation of the formyl peptide receptors and reorganization of the actin cytoskeleton (By similarity). Has high affinity for Ca(2+) and can bind up to eight Ca(2+) ions (By similarity). Displays Ca(2+)-dependent binding to phospholipid membranes (PubMed:3020049). Plays a role in the formation of phagocytic cups and phagosomes. Plays a role in phagocytosis by mediating the Ca(2+)-dependent interaction between phagosomes and the actin cytoskeleton (By similarity). In the context of antitumor immunity, interacts with FPR1 on dendritic cells allowing for tumor-associated antigens uptake and cross-presentation to T cells to mount an antitumor specific T cell response

Protein Sequence

10 MAMVSEFLKQ 20 ACYIEKQEQE 30 YVQAVKSYKG 40 GPGSAVSPYP 50 SFNPSSDVAA 60 LHKAIMVKGV 70 DEATIIDILT 80 KRTNAQRQQI 90 KAAYLQETGK 100 PLDETLKKAL 110 TGHLEEVVLA 120 MLKTPAQFDA 130 DELRAAMKGL 140 GTDEDTLIEI 150 LTTRSNQQIR 160 EITRVYREEL 170 KRDLAKDITS 180 DTSGDFRNAL 190 LALAKGDRCE 200 DMSVNQDLAD 210 TDARALYEAG 220 ERRKGTDVNV 230 FNTILTTRSY 240 PHLRKVFQNY 250 RKYSQHDMNK 260 ALDLELKGDI 270 EKCLTTIVKC 280 ATSTPAFFAE 290 KLYEAMKGAG 300 TRHKTLIRIM 310 VSRSEIDMNE 320 IKVFYQKKYG 330 IPLCQAILDE 340 TKGDYEKILV ALCGGN

Gene Ontology

Classification GO ID Description
Biological Process GO:0090050 positive regulation of cell migration involved in sprouting angiogenesis
Cellular Component GO:0005884 actin filament
Cellular Component GO:0016324 apical plasma membrane
Cellular Component GO:0016323 basolateral plasma membrane
Cellular Component GO:0009986 cell surface
Cellular Component GO:0001533 cornified envelope
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0031901 early endosome membrane
Cellular Component GO:0005768 endosome
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0016328 lateral plasma membrane
Cellular Component GO:0042629 mast cell granule
Cellular Component GO:0031966 mitochondrial membrane
Cellular Component GO:0031514 motile cilium
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0001891 phagocytic cup
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:0042383 sarcolemma
Cellular Component GO:0097060 synaptic membrane
Cellular Component GO:0012506 vesicle membrane
Molecular Function GO:0005509 calcium ion binding
Molecular Function GO:0005544 calcium-dependent phospholipid binding
Molecular Function GO:0048306 calcium-dependent protein binding
Molecular Function GO:1990814 DNA/DNA annealing activity
Molecular Function GO:0036121 double-stranded DNA helicase activity
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0008289 lipid binding
Molecular Function GO:0001786 phosphatidylserine binding
Molecular Function GO:0019834 phospholipase A2 inhibitor activity
Molecular Function GO:0005543 phospholipid binding
Molecular Function GO:0003697 single-stranded DNA binding
Biological Process GO:0030036 actin cytoskeleton organization
Biological Process GO:0002250 adaptive immune response
Biological Process GO:0046632 alpha-beta T cell differentiation
Biological Process GO:0050482 arachidonate secretion
Biological Process GO:0007166 cell surface receptor signaling pathway
Biological Process GO:0071385 cellular response to glucocorticoid stimulus
Biological Process GO:0070301 cellular response to hydrogen peroxide
Biological Process GO:0035924 cellular response to vascular endothelial growth factor stimulus
Biological Process GO:0031018 endocrine pancreas development
Biological Process GO:0044849 estrous cycle
Biological Process GO:0007187 G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger
Biological Process GO:0042063 gliogenesis
Biological Process GO:0071621 granulocyte chemotaxis
Biological Process GO:0070365 hepatocyte differentiation
Biological Process GO:0006954 inflammatory response
Biological Process GO:0045087 innate immune response
Biological Process GO:0030073 insulin secretion
Biological Process GO:0030216 keratinocyte differentiation
Biological Process GO:0002548 monocyte chemotaxis
Biological Process GO:0014839 myoblast migration involved in skeletal muscle regeneration
Biological Process GO:0045920 negative regulation of exocytosis
Biological Process GO:0032717 negative regulation of interleukin-8 production
Biological Process GO:0050709 negative regulation of protein secretion
Biological Process GO:0045629 negative regulation of T-helper 2 cell differentiation
Biological Process GO:0042119 neutrophil activation
Biological Process GO:0097350 neutrophil clearance
Biological Process GO:0001780 neutrophil homeostasis
Biological Process GO:0018149 peptide cross-linking
Biological Process GO:0006909 phagocytosis
Biological Process GO:0043065 positive regulation of apoptotic process
Biological Process GO:1900087 positive regulation of G1/S transition of mitotic cell cycle
Biological Process GO:0032743 positive regulation of interleukin-2 production
Biological Process GO:0033031 positive regulation of neutrophil apoptotic process
Biological Process GO:0031394 positive regulation of prostaglandin biosynthetic process
Biological Process GO:0042102 positive regulation of T cell proliferation
Biological Process GO:0045627 positive regulation of T-helper 1 cell differentiation
Biological Process GO:0031340 positive regulation of vesicle fusion
Biological Process GO:0090303 positive regulation of wound healing
Biological Process GO:0070459 prolactin secretion
Biological Process GO:0030850 prostate gland development
Biological Process GO:0042127 regulation of cell population proliferation
Biological Process GO:0008360 regulation of cell shape
Biological Process GO:0046883 regulation of hormone secretion
Biological Process GO:0050727 regulation of inflammatory response
Biological Process GO:0032652 regulation of interleukin-1 production
Biological Process GO:0002685 regulation of leukocyte migration
Biological Process GO:0032355 response to estradiol
Biological Process GO:0051384 response to glucocorticoid
Biological Process GO:0009725 response to hormone
Biological Process GO:0070555 response to interleukin-1
Biological Process GO:1904373 response to kainic acid
Biological Process GO:0043434 response to peptide hormone
Biological Process GO:0010165 response to X-ray
Biological Process GO:0009410 response to xenobiotic stimulus
Biological Process GO:0007165 signal transduction

Reference

[1] Sheng L, Xu H, Wang Y, Ni J, Xiang T et al.. Systematic analysis of lysine lactylation in nucleus pulposus cells.. iScience 27(11):111157. 2024 Nov 15. PMID: 39524337.